Updated on 2025/08/06

写真a

 
Fujita Naonobu
 
Organization
Institute of Integrated Research Cell Biology Center Associate Professor
Title
Associate Professor
Homepage
https://kaken.nii.ac.jp/d/r/00506496.ja.html
External link

News & Topics

  • 蛹期に備えて幼虫脂肪体のオートファジーは抑制される

    2022/03/23

    Languages： Japanese

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    要点-オートファジーによる任意のタンパク質の分解を生細胞で解析できる新たなシステムを開発-ショウジョウバエの幼虫の最終期には、哺乳動物の肝臓と脂肪組織にあたる脂肪体で、タンパク質などの分解を担うリソソームの機能が低下することを発見-多様な疾患の分子標的となりうるオートファジー・リソソーム機能の調節メ

  • 筋細胞内に管状のリソソームネットワークを発見 超高齢化社会の課題である筋機能の維持に向けた新たな知見

    2020/10/20

    Languages： Japanese

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    要点-ショウジョウバエの筋細胞が作り変えられる際に、オートファジーに依存して、リソソームが管状のネットワークを形成する現象を発見-管状ネットワークの形成により、筋細胞の広い範囲でリソソームが同調する-超高齢化社会の課題である筋機能維持へ向けて新たな知見を提供すると期待[image:筋細胞内の管状リソ

Degree

  • 理学博士

Research Interests

  • Lysosome

  • T-tubule

  • タンパク質分解

  • オートファジー

  • Drosophila melanogaster

  • muscle cell

  • Nephrocyte

  • ユビキチン

Research Areas

  • Life Science / Cell biology

Education

  • The Graduate University for Advanced Studies   School of Life Science   Department of Genetics

    2005.4 - 2008.3

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  • Tokyo University of Agriculture and Technology

    2003.4 - 2005.3

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  • Tokyo University of Agriculture and Technology   Faculty of Agriculture   Department of Applied Biological Science

    1999.4 - 2003.3

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Research History

  • Institute of Science Tokyo   Cell Biology Center, Institute of Integrated Research   Associate Professor

    2024.10

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  • Tokyo Institute of Technology   Cell Biology Center, Institute of Innovative Research   Associate Professor

    2019.3

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  • Japan Science and Technology Agency

    2018.10 - 2022.3

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  • 東北大学大学院   生命科学研究科   助教

    2015.5 - 2019.2

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  • University of California, San Diego

    2012.3 - 2015.4

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  • 大阪大学大学院   生命機能研究科   助教

    2010.4 - 2012.2

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  • Osaka University   Research Institute for Microbial Diseases

    2008.4 - 2010.3

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Papers

  • Linear ubiquitination triggers Amph-mediated T-tubule biogenesis

    Kohei Kawaguchi, Yutaro Hama, Harunori Yoshikawa, Kohei Nishino, Kazuki Morimoto, Tsuyoshi Nakamura, Michiko Koizumi, Yuriko Sakamaki, Kota Abe, Soichiro Kakuta, Koichiro Ichimura, Fumiyo Ikeda, Hidetaka Kosako, Naonobu Fujita

    bioRxiv   2025.4

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    Publisher：Cold Spring Harbor Laboratory  

    Abstract

    T-tubules are specialized invaginations of the plasma membrane essential for muscle contraction. While their physiological importance is well established, the mechanisms underlying T-tubule formation remain elusive. Here, we identify LUBEL/RNF31, a ubiquitin E3 ligase responsible for linear (M1-linked) ubiquitination, as a key regulator of T-tubule biogenesis through proximity proteomics and RNAi screening inDrosophila. Loss of LUBEL leads to the formation of Amphiphysin (Amph)-positive membrane sheets instead of tubular networks in muscle cells. Mechanistically, the ubiquitin ligase activity of LUBEL, and direct interaction with Amph, a BAR domain protein involved in membrane tubule extension, are crucial for proper T-tubule morphology. LUBEL and M1-linked ubiquitin chains assemble into condensates on membranes, facilitating Amph-mediated membrane tubulation. Notably, the Amph-LUBEL/RNF31 interaction is evolutionarily conserved across a broad range of species, underscoring a fundamental role for linear ubiquitination in membrane remodeling. Our findings uncover a previously unrecognized role for linear ubiquitination in membrane deformation driven by BAR domain proteins.

    DOI： 10.1101/2025.04.03.646909

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  • Transcriptional Dynamics Uncover the Role of BNIP3 in Mitophagy during Muscle Remodeling in Drosophila

    Hiroki Taoka, Tadayoshi Murakawa, Kohei Kawaguchi, Michiko Koizumi, Tatsuya Kaminishi, Yuriko Sakamaki, Kaori Tanaka, Akihito Harada, Keiichi Inoue, Tomotake Kanki, Yasuyuki Ohkawa, Naonobu Fujita

    eLife   https://doi.org/10.7554/eLife.105834.1   2025.3

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    Publisher：eLife Sciences Publications, Ltd  

    Abstract

    Differentiated muscle cells contain myofibrils and well-organized organelles, enabling powerful contractions. Muscle cell reorganization occurs in response to various physiological stimuli; however, the mechanisms behind this remodeling remain enigmatic due to the lack of a genetically trackable system. Previously, we reported that a subset of larval muscle cells is remodeled into adult abdominal muscle through an autophagy-dependent mechanism in Drosophila. To unveil the underlying mechanisms of this remodeling, we performed a comparative time-course RNA-seq analysis of isolated muscle cells with or without autophagy. It revealed both transcriptional dynamics independent of autophagy and highlighted the significance of BNIP3-mediated mitophagy in muscle remodeling. Mechanistically, we found that BNIP3 recruits autophagic machinery to mitochondria through its LC3-interacting (LIR) motif and minimal essential region (MER), which interact with Atg8a and Atg18a, respectively. Loss of BNIP3 leads to a substantial accumulation of larval mitochondria, ultimately impairing muscle remodeling. In summary, this study demonstrates that BNIP3-dependent mitophagy is critical for orchestrating the dynamic process of muscle remodeling.

    DOI： 10.7554/elife.105834.1

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  • Shaping transverse-tubules: central mechanisms that play a role in the cytosol zoning for muscle contraction. International journal

    Kohei Kawaguchi, Naonobu Fujita

    Journal of biochemistry   175 ( 2 )   125 - 131   2024.2

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    Language：English   Publishing type：Research paper (scientific journal)  

    A transverse-tubule (T-tubule) is an invagination of the plasma membrane penetrating deep into muscle cells. An extensive membrane network of T-tubules is crucial for rapid and synchronized signal transmission from the cell surface to the entire sarcoplasmic reticulum for Ca2+ release, leading to muscle contraction. T-tubules are also indispensable for the formation and positioning of other muscle organelles. Their structure and physiological roles are relatively well established; however, the mechanisms shaping T-tubules require further elucidation. Centronuclear myopathy (CNM), an inherited muscular disorder, accompanies structural defects in T-tubules. Membrane traffic-related genes, including MTM1 (Myotubularin 1), DNM2 (Dynamin 2), and BIN1 (Bridging Integrator-1), were identified as causative genes of CNM. In addition, causative genes for other muscle diseases are also reported to be involved in the formation and maintenance of T-tubules. This review summarizes current knowledge on the mechanisms of how T-tubule formation and maintenance is regulated.

    DOI： 10.1093/jb/mvad083

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  • PI(4,5)P 2 role in Transverse-tubule membrane formation and muscle function. International journal

    Naonobu Fujita, Shravan Girada, Georg Vogler, Rolf Bodmer, Amy A Kiger

    bioRxiv : the preprint server for biology   2024.1

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    Language：English   Publishing type：Research paper (scientific journal)  

    UNLABELLED: Transverse (T)-tubules - vast, tubulated domains of the muscle plasma membrane - are critical to maintain healthy skeletal and heart contractions. How the intricate T-tubule membranes are formed is not well understood, with challenges to systematically interrogate in muscle. We established the use of intact Drosophila larval body wall muscles as an ideal system to discover mechanisms that sculpt and maintain the T-tubule membrane network. A muscle-targeted genetic screen identified specific phosphoinositide lipid regulators necessary for T-tubule organization and muscle function. We show that a PI4KIIIα - Skittles/PIP5K pathway is needed for T-tubule localized PI(4)P to PI(4,5)P 2 synthesis, T-tubule organization, calcium regulation, and muscle and heart rate functions. Muscles deficient for PI4KIIIα or Amphiphysin , the homolog of human BIN1 , similarly exhibited specific loss of transversal T-tubule membranes and dyad junctions, yet retained longitudinal membranes and the associated dyads. Our results highlight the power of live muscle studies, uncovering distinct mechanisms and functions for sub-compartments of the T-tubule network relevant to human myopathy. SUMMARY: T-tubules - vast, tubulated domains of the muscle plasma membrane - are critical to maintain skeletal and heart contractions. Fujita et al . establish genetic screens and assays in intact Drosophila muscles that uncover PI(4,5)P 2 regulation critical for T-tubule maintenance and function. KEY FINDINGS: PI4KIIIα is required for muscle T-tubule formation and larval mobility. A PI4KIIIα-Sktl pathway promotes PI(4)P and PI(4,5)P 2 function at T-tubules. PI4KIIIα is necessary for calcium dynamics and transversal but not longitudinal dyads. Disruption of PI(4,5)P 2 function in fly heart leads to fragmented T-tubules and abnormal heart rate.

    DOI： 10.1101/2024.01.31.578124

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  • Neuronal MML-1/MXL-2 regulates systemic aging via glutamate transporter and cell nonautonomous autophagic and peroxidase activity. International journal

    Tatsuya Shioda, Ittetsu Takahashi, Kensuke Ikenaka, Naonobu Fujita, Tomotake Kanki, Toshihiko Oka, Hideki Mochizuki, Adam Antebi, Tamotsu Yoshimori, Shuhei Nakamura

    Proceedings of the National Academy of Sciences of the United States of America   120 ( 39 )   e2221553120   2023.9

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    Language：English   Publishing type：Research paper (scientific journal)  

    Accumulating evidence has demonstrated the presence of intertissue-communication regulating systemic aging, but the underlying molecular network has not been fully explored. We and others previously showed that two basic helix-loop-helix transcription factors, MML-1 and HLH-30, are required for lifespan extension in several longevity paradigms, including germlineless Caenorhabditis elegans. However, it is unknown what tissues these factors target to promote longevity. Here, using tissue-specific knockdown experiments, we found that MML-1 and its heterodimer partners MXL-2 and HLH-30 act primarily in neurons to extend longevity in germlineless animals. Interestingly, however, the downstream cascades of MML-1 in neurons were distinct from those of HLH-30. Neuronal RNA interference (RNAi)-based transcriptome analysis revealed that the glutamate transporter GLT-5 is a downstream target of MML-1 but not HLH-30. Furthermore, the MML-1-GTL-5 axis in neurons is critical to prevent an age-dependent collapse of proteostasis and increased oxidative stress through autophagy and peroxidase MLT-7, respectively, in long-lived animals. Collectively, our study revealed that systemic aging is regulated by a molecular network involving neuronal MML-1 function in both neural and peripheral tissues.

    DOI： 10.1073/pnas.2221553120

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  • A Drosophila toolkit for HA-tagged proteins unveils a block in autophagy flux in the last instar larval fat body Reviewed International journal

    Tadayoshi Murakawa, Tsuyoshi Nakamura, Kohei Kawaguchi, Futoshi Murayama, Ning Zhao, Timothy J. Stasevich, Hiroshi Kimura, Naonobu Fujita

    Development   149 ( 6 )   2022.3

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    Language：English   Publishing type：Research paper (scientific journal)   Publisher：The Company of Biologists  

    ABSTRACT

    For in vivo functional analysis of a protein of interest (POI), multiple transgenic strains with a POI that harbors different tags are needed but generation of these strains is still labor-intensive work. To overcome this, we have developed a versatile Drosophila toolkit with a genetically encoded single-chain variable fragment for the HA epitope tag: ‘HA Frankenbody’. This system allows various analyses of HA-tagged POI in live tissues by simply crossing an HA Frankenbody fly with an HA-tagged POI fly. Strikingly, the GFP-mCherry tandem fluorescent-tagged HA Frankenbody revealed a block in autophagic flux and an accumulation of enlarged autolysosomes in the last instar larval and prepupal fat body. Mechanistically, lysosomal activity was downregulated at this stage, and endocytosis, but not autophagy, was indispensable for the swelling of lysosomes. Furthermore, forced activation of lysosomes by fat body-targeted overexpression of Mitf, the single MiTF/TFE family gene in Drosophila, suppressed the lysosomal swelling and resulted in pupal lethality. Collectively, we propose that downregulated lysosomal function in the fat body plays a role in the metamorphosis of Drosophila.

    DOI： 10.1242/dev.200243

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  • An autophagy-dependent tubular lysosomal network synchronizes degradative activity required for muscle remodeling. Reviewed International journal

    Tadayoshi Murakawa, Amy A Kiger, Yuriko Sakamaki, Mitsunori Fukuda, Naonobu Fujita

    Journal of cell science   133 ( 21 )   2020.11

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    Language：English   Publishing type：Research paper (scientific journal)  

    Lysosomes are compartments for the degradation of both endocytic and autophagic cargoes. The shape of lysosomes changes with cellular degradative demands; however, there is limited knowledge about the mechanisms or significance that underlies distinct lysosomal morphologies. Here, we found an extensive tubular autolysosomal network in Drosophila abdominal muscle remodeling during metamorphosis. The tubular network transiently appeared and exhibited the capacity to degrade autophagic cargoes. The tubular autolysosomal network was uniquely marked by the autophagic SNARE protein Syntaxin17 and its formation depended on both autophagic flux and degradative function, with the exception of the Atg12 and Atg8 ubiquitin-like conjugation systems. Among ATG-deficient mutants, the efficiency of lysosomal tubulation correlated with the phenotypic severity in muscle remodeling. The lumen of the tubular network was continuous and homogeneous across a broad region of the remodeling muscle. Altogether, we revealed that the dynamic expansion of a tubular autolysosomal network synchronizes the abundant degradative activity required for developmentally regulated muscle remodeling.

    DOI： 10.1242/jcs.248336

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  • Comprehensive knockout analysis of the Rab family GTPases in epithelial cells. Reviewed International journal

    Yuta Homma, Riko Kinoshita, Yoshihiko Kuchitsu, Paulina S Wawro, Soujiro Marubashi, Mai E Oguchi, Morié Ishida, Naonobu Fujita, Mitsunori Fukuda

    The Journal of cell biology   218 ( 6 )   2035 - 2050   2019.6

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    Language：English   Publishing type：Research paper (scientific journal)  

    The Rab family of small GTPases comprises the largest number of proteins (∼60 in mammals) among the regulators of intracellular membrane trafficking, but the precise function of many Rabs and the functional redundancy and diversity of Rabs remain largely unknown. Here, we generated a comprehensive collection of knockout (KO) MDCK cells for the entire Rab family. We knocked out closely related paralogs simultaneously (Rab subfamily knockout) to circumvent functional compensation and found that Rab1A/B and Rab5A/B/C are critical for cell survival and/or growth. In addition, we demonstrated that Rab6-KO cells lack the basement membrane, likely because of the inability to secrete extracellular matrix components. Further analysis revealed the general requirement of Rab6 for secretion of soluble cargos. Transport of transmembrane cargos to the plasma membrane was also significantly delayed in Rab6-KO cells, but the phenotype was relatively mild. Our Rab-KO collection, which shares the same background, would be a valuable resource for analyzing a variety of membrane trafficking events.

    DOI： 10.1083/jcb.201810134

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  • Rab7 knockout unveils regulated autolysosome maturation induced by glutamine starvation. Reviewed International journal

    Yoshihiko Kuchitsu, Yuta Homma, Naonobu Fujita, Mitsunori Fukuda

    Journal of cell science   131 ( 7 )   2018.4

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    Language：English   Publishing type：Research paper (scientific journal)   Publisher：Company of Biologists Ltd  

    DOI： 10.1242/jcs.215442

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  • Genetic screen in Drosophila muscle identifies autophagy-mediated T-tubule remodeling and a Rab2 role in autophagy. Reviewed International journal

    Naonobu Fujita, Wilson Huang, Tzu-Han Lin, Jean-Francois Groulx, Steve Jean, Jen Nguyen, Yoshihiko Kuchitsu, Ikuko Koyama-Honda, Noboru Mizushima, Mitsunori Fukuda, Amy A Kiger

    eLife   6   2017.1

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    DOI： 10.7554/eLife.23367

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  • Atg9A trafficking through the recycling endosomes is required for autophagosome formation. Reviewed International journal

    Kenta Imai, Feike Hao, Naonobu Fujita, Yasuhiro Tsuji, Yukako Oe, Yasuhiro Araki, Maho Hamasaki, Takeshi Noda, Tamotsu Yoshimori

    Journal of cell science   129 ( 20 )   3781 - 3791   2016.10

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    DOI： 10.1242/jcs.196196

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  • Differing susceptibility to autophagic degradation of two LC3-binding proteins: SQSTM1/p62 and TBC1D25/OATL1. Reviewed International journal

    Satoshi Hirano, Takefumi Uemura, Hiromichi Annoh, Naonobu Fujita, Satoshi Waguri, Takashi Itoh, Mitsunori Fukuda

    Autophagy   12 ( 2 )   312 - 26   2016

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    Language：English   Publishing type：Research paper (scientific journal)  

    DOI： 10.1080/15548627.2015.1124223

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  • Jam1a-Jam2a interactions regulate haematopoietic stem cell fate through Notch signalling. Reviewed International journal

    Isao Kobayashi, Jingjing Kobayashi-Sun, Albert D Kim, Claire Pouget, Naonobu Fujita, Toshio Suda, David Traver

    Nature   512 ( 7514 )   319 - 23   2014.8

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    Language：English   Publishing type：Research paper (scientific journal)  

    DOI： 10.1038/nature13623

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  • The parasitophorous vacuole membrane of Toxoplasma gondii is targeted for disruption by ubiquitin-like conjugation systems of autophagy. Reviewed International journal

    Jayoung Choi, Sunmin Park, Scott B Biering, Elizabeth Selleck, Catherine Y Liu, Xin Zhang, Naonobu Fujita, Tatsuya Saitoh, Shizuo Akira, Tamotsu Yoshimori, L David Sibley, Seungmin Hwang, Herbert W Virgin

    Immunity   40 ( 6 )   924 - 35   2014.6

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    Language：English   Publishing type：Research paper (scientific journal)  

    DOI： 10.1016/j.immuni.2014.05.006

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  • Autophagy in the placenta of women with hypertensive disorders in pregnancy

    Akaishi, R., Yamada, T., Nakabayashi, K., Nishihara, H., Furuta, I., Kojima, T., Morikawa, M., Fujita, N., Minakami, H.

    Placenta   35 ( 12 )   2014

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    Publishing type：Research paper (scientific journal)  

    DOI： 10.1016/j.placenta.2014.10.009

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  • Recruitment of the autophagic machinery to endosomes during infection is mediated by ubiquitin. Reviewed International journal

    Naonobu Fujita, Eiji Morita, Takashi Itoh, Atsushi Tanaka, Megumi Nakaoka, Yuki Osada, Tetsuo Umemoto, Tatsuya Saitoh, Hitoshi Nakatogawa, Shouhei Kobayashi, Tokuko Haraguchi, Jun-Lin Guan, Kazuhiro Iwai, Fuminori Tokunaga, Kazunobu Saito, Koutaro Ishibashi, Shizuo Akira, Mitsunori Fukuda, Takeshi Noda, Tamotsu Yoshimori

    The Journal of cell biology   203 ( 1 )   115 - 28   2013.10

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    DOI： 10.1083/jcb.201304188

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  • Autophagosomes form at ER-mitochondria contact sites. Reviewed International journal

    Maho Hamasaki, Nobumichi Furuta, Atsushi Matsuda, Akiko Nezu, Akitsugu Yamamoto, Naonobu Fujita, Hiroko Oomori, Takeshi Noda, Tokuko Haraguchi, Yasushi Hiraoka, Atsuo Amano, Tamotsu Yoshimori

    Nature   495 ( 7441 )   389 - 93   2013.3

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    Language：English   Publishing type：Research paper (scientific journal)  

    DOI： 10.1038/nature11910

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  • Impaired autophagy by soluble endoglin, under physiological hypoxia in early pregnant period, is involved in poor placentation in preeclampsia. Reviewed International journal

    Akitoshi Nakashima, Mikiko Yamanaka-Tatematsu, Naonobu Fujita, Keiichi Koizumi, Tomoko Shima, Toshiko Yoshida, Toshio Nikaido, Aikou Okamoto, Tamotsu Yoshimori, Shigeru Saito

    Autophagy   9 ( 3 )   303 - 16   2013.3

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    Language：English   Publishing type：Research paper (scientific journal)  

    DOI： 10.4161/auto.22927

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  • Autophagy induced by HIF1α overexpression supports trophoblast invasion by supplying cellular energy. Reviewed International journal

    Mikiko Yamanaka-Tatematsu, Akitoshi Nakashima, Naonobu Fujita, Tomoko Shima, Tamotsu Yoshimori, Shigeru Saito

    PloS one   8 ( 10 )   e76605   2013

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    Language：English   Publishing type：Research paper (scientific journal)  

    DOI： 10.1371/journal.pone.0076605

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  • Inhibition of autophagy potentiates the antitumor effect of the multikinase inhibitor sorafenib in hepatocellular carcinoma. Reviewed International journal

    Satoshi Shimizu, Tetsuo Takehara, Hayato Hikita, Takahiro Kodama, Hinako Tsunematsu, Takuya Miyagi, Atsushi Hosui, Hisashi Ishida, Tomohide Tatsumi, Tatsuya Kanto, Naoki Hiramatsu, Naonobu Fujita, Tamotsu Yoshimori, Norio Hayashi

    International journal of cancer   131 ( 3 )   548 - 57   2012.8

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    Language：English   Publishing type：Research paper (scientific journal)  

    DOI： 10.1002/ijc.26374

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  • Autophagy guards against cisplatin-induced acute kidney injury. Reviewed International journal

    Atsushi Takahashi, Tomonori Kimura, Yoshitsugu Takabatake, Tomoko Namba, Junya Kaimori, Harumi Kitamura, Isao Matsui, Fumio Niimura, Taiji Matsusaka, Naonobu Fujita, Tamotsu Yoshimori, Yoshitaka Isaka, Hiromi Rakugi

    The American journal of pathology   180 ( 2 )   517 - 25   2012.2

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    DOI： 10.1016/j.ajpath.2011.11.001

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  • Three-Axis Model for Atg Recruitment in Autophagy against Salmonella. Reviewed International journal

    Takeshi Noda, Shun Kageyama, Naonobu Fujita, Tamotsu Yoshimori

    International journal of cell biology   2012   389562 - 389562   2012

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    Salmonella enterica serovar Typhimurium enter epithelial cells and take up residence there. Within epithelial cells, a portion of the bacteria are surrounded by an autophagosome-like double-membrane structure, and they are still residing within the Salmonella-containing vacuole (SCV). In this paper, we will discuss how the autophagy machinery is recruited in proximity to Salmonella. The formation of this double membrane requires Atg9L1 and FIP200; these proteins are important for autophagy-specific recruitment of the PI3-kinase complex. In the absence of Atg9L1, FIP200, and PI3-kinase activity, LC3 is still recruited to the vicinity of Salmonella. We propose a novel model in which the mechanism of LC3 recruitment is separate from the generation of the isolation membrane. There exist at least three axes in Atg recruitment: ULK1 complex, Atg9L1, and Atg16L complex.

    DOI： 10.1155/2012/389562

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  • Atg16L2, a novel isoform of mammalian Atg16L that is not essential for canonical autophagy despite forming an Atg12–5-16L2 complex. Reviewed International journal

    Koutaro Ishibashi, Naonobu Fujita, Eiko Kanno, Hiroko Omori, Tamotsu Yoshimori, Takashi Itoh, Mitsunori Fukuda

    Autophagy   7 ( 12 )   1500 - 13   2011.12

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    Language：English   Publishing type：Research paper (scientific journal)  

    DOI： 10.4161/auto.7.12.18025

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  • Dysfunction of autophagy participates in vacuole formation and cell death in cells replicating hepatitis C virus. Reviewed International journal

    Shuhei Taguwa, Hiroto Kambara, Naonobu Fujita, Takeshi Noda, Tamotsu Yoshimori, Kazuhiko Koike, Kohji Moriishi, Yoshiharu Matsuura

    Journal of virology   85 ( 24 )   13185 - 94   2011.12

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    DOI： 10.1128/JVI.06099-11

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  • Ubiquitination-mediated autophagy against invading bacteria. Reviewed International journal

    Naonobu Fujita, Tamotsu Yoshimori

    Current opinion in cell biology   23 ( 4 )   492 - 7   2011.8

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    DOI： 10.1016/j.ceb.2011.03.003

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  • Autophagosomes can support Yersinia pseudotuberculosis replication in macrophages. Reviewed International journal

    Kevin Moreau, Sandra Lacas-Gervais, Naonobu Fujita, Florent Sebbane, Tamotsu Yoshimori, Michel Simonet, Frank Lafont

    Cellular microbiology   12 ( 8 )   1108 - 23   2010.8

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    DOI： 10.1111/j.1462-5822.2010.01456.x

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  • Regulation of dsDNA-induced innate immune responses by membrane trafficking. Reviewed International journal

    Tatsuya Saitoh, Naonobu Fujita, Tamotsu Yoshimori, Shizuo Akira

    Autophagy   6 ( 3 )   430 - 2   2010.4

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    Language：English   Publishing type：Research paper (scientific journal)  

    DOI： 10.4161/auto.6.3.11611

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  • Combinational soluble N-ethylmaleimide-sensitive factor attachment protein receptor proteins VAMP8 and Vti1b mediate fusion of antimicrobial and canonical autophagosomes with lysosomes. Reviewed International journal

    Nobumichi Furuta, Naonobu Fujita, Takeshi Noda, Tamotsu Yoshimori, Atsuo Amano

    Molecular biology of the cell   21 ( 6 )   1001 - 10   2010.3

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    Language：English   Publishing type：Research paper (scientific journal)  

    DOI： 10.1091/mbc.E09-08-0693

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  • Electron tomography reveals the endoplasmic reticulum as a membrane source for autophagosome formation. Reviewed International journal

    Mitsuko Hayashi-Nishino, Naonobu Fujita, Takeshi Noda, Akihito Yamaguchi, Tamotsu Yoshimori, Akitsugu Yamamoto

    Autophagy   6 ( 2 )   301 - 3   2010.2

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    Language：English   Publishing type：Research paper (scientific journal)   Publisher：Informa UK Limited  

    The origin and source of autophagosomal membranes are long-standing questions. By electron microscopy, we show that the endoplasmic reticulum (ER) associates with early autophagic structures called isolation membranes (IM) or phagophores in mammalian culture cells. Overexpression of a mutant of Atg4B, which causes defects in autophagosome formation, caused accumulation of ER-IM complexes. Electron tomography revealed the ER-IM complex as a subdomain of the ER forming a cradle encircling the IM, and showed that both ER and isolation membranes are interconnected.

    DOI： 10.4161/auto.6.2.11134

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  • Atg9a controls dsDNA-driven dynamic translocation of STING and the innate immune response. Reviewed International journal

    Tatsuya Saitoh, Naonobu Fujita, Takuya Hayashi, Keigo Takahara, Takashi Satoh, Hanna Lee, Kohichi Matsunaga, Shun Kageyama, Hiroko Omori, Takeshi Noda, Naoki Yamamoto, Taro Kawai, Ken Ishii, Osamu Takeuchi, Tamotsu Yoshimori, Shizuo Akira

    Proceedings of the National Academy of Sciences of the United States of America   106 ( 49 )   20842 - 6   2009.12

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    DOI： 10.1073/pnas.0911267106

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  • A subdomain of the endoplasmic reticulum forms a cradle for autophagosome formation. Reviewed International journal

    Mitsuko Hayashi-Nishino, Naonobu Fujita, Takeshi Noda, Akihito Yamaguchi, Tamotsu Yoshimori, Akitsugu Yamamoto

    Nature cell biology   11 ( 12 )   1433 - 7   2009.12

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    DOI： 10.1038/ncb1991

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  • Differential involvement of Atg16L1 in Crohn disease and canonical autophagy: analysis of the organization of the Atg16L1 complex in fibroblasts. Reviewed International journal

    Naonobu Fujita, Tatsuya Saitoh, Shun Kageyama, Shizuo Akira, Takeshi Noda, Tamotsu Yoshimori

    The Journal of biological chemistry   284 ( 47 )   32602 - 9   2009.11

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    DOI： 10.1074/jbc.M109.037671

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  • Autophagy and the Endoplasmic Reticulum Invited Reviewed

    M. Hayashi-Nishino, N. Fujita, T. Noda, A. Yamaguchi, T. Yoshimori, A. Yamamoto

    2009.9

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  • [Regulation of inflammation by autophagy]. Reviewed

    Tatsuya Saitoh, Fujita Naonobu, Tamotsu Yoshimori, Shizuo Akira

    Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme   54 ( 8 Suppl )   1119 - 24   2009.6

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  • Atg4B(C74A) hampers autophagosome closure: a useful protein for inhibiting autophagy. Reviewed International journal

    Naonobu Fujita, Takeshi Noda, Tamotsu Yoshimori

    Autophagy   5 ( 1 )   88 - 9   2009.1

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    DOI： 10.1091/mbc.E08-03-0312

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  • Monitoring autophagy in mammalian cultured cells through the dynamics of LC3. Reviewed International journal

    Shunsuke Kimura, Naonobu Fujita, Takeshi Noda, Tamotsu Yoshimori

    Methods in enzymology   452   1 - 12   2009

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    DOI： 10.1016/S0076-6879(08)03601-X

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  • The late stages of autophagy : how does the end begin?

    NODA T.

    Cell Death Differ   16 ( 7 )   984 - 990   2009

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  • [Autophagy and innate immunity]. Reviewed

    Tatsuya Saitoh, Naonobu Fujita, Tamotsu Yoshimori, Shizuo Akira

    Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme   53 ( 16 Suppl )   2279 - 85   2008.12

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  • [Molecular mechanism of autophagosome formation in mammalian cells]. Reviewed

    Naonobu Fujita, Kohichi Matsunaga, Takeshi Noda, Tamotsu Yoshimori

    Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme   53 ( 16 Suppl )   2106 - 10   2008.12

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  • Loss of the autophagy protein Atg16L1 enhances endotoxin-induced IL-1beta production. Reviewed International journal

    Tatsuya Saitoh, Naonobu Fujita, Myoung Ho Jang, Satoshi Uematsu, Bo-Gie Yang, Takashi Satoh, Hiroko Omori, Takeshi Noda, Naoki Yamamoto, Masaaki Komatsu, Keiji Tanaka, Taro Kawai, Tohru Tsujimura, Osamu Takeuchi, Tamotsu Yoshimori, Shizuo Akira

    Nature   456 ( 7219 )   264 - 8   2008.11

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    DOI： 10.1038/nature07383

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  • An Atg4B mutant hampers the lipidation of LC3 paralogues and causes defects in autophagosome closure. Reviewed International journal

    Naonobu Fujita, Mitsuko Hayashi-Nishino, Hiromi Fukumoto, Hiroko Omori, Akitsugu Yamamoto, Takeshi Noda, Tamotsu Yoshimori

    Molecular biology of the cell   19 ( 11 )   4651 - 9   2008.11

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    DOI： 10.1091/mbc.E08-03-0312

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  • Golgi-resident small GTPase Rab33B interacts with Atg16L and modulates autophagosome formation. Reviewed International journal

    Takashi Itoh, Naonobu Fujita, Eiko Kanno, Akitsugu Yamamoto, Tamotsu Yoshimori, Mitsunori Fukuda

    Molecular biology of the cell   19 ( 7 )   2916 - 25   2008.7

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    DOI： 10.1091/mbc.E07-12-1231

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  • The Ubi brothers reunited. Reviewed International journal

    Takeshi Noda, Naonobu Fujita, Tamotsu Yoshimori

    Autophagy   4 ( 4 )   540 - 1   2008.5

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  • The Atg16L complex specifies the site of LC3 lipidation for membrane biogenesis in autophagy. Reviewed International journal

    Naonobu Fujita, Takashi Itoh, Hiroko Omori, Mitsunori Fukuda, Takeshi Noda, Tamotsu Yoshimori

    Molecular biology of the cell   19 ( 5 )   2092 - 100   2008.5

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    DOI： 10.1091/mbc.E07-12-1257

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  • The relative contribution of mannose salvage pathways to glycosylation in PMI-deficient mouse embryonic fibroblast cells. Reviewed International journal

    Naonobu Fujita, Ayako Tamura, Aya Higashidani, Takashi Tonozuka, Hudson H Freeze, Atsushi Nishikawa

    The FEBS journal   275 ( 4 )   788 - 98   2008.2

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    DOI： 10.1111/j.1742-4658.2008.06246.x

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  • Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition)1. International journal

    Daniel J Klionsky, Amal Kamal Abdel-Aziz, Sara Abdelfatah, Mahmoud Abdellatif, Asghar Abdoli, Steffen Abel, Hagai Abeliovich, Marie H Abildgaard, Yakubu Princely Abudu, Abraham Acevedo-Arozena, Iannis E Adamopoulos, Khosrow Adeli, Timon E Adolph, Annagrazia Adornetto, Elma Aflaki, Galila Agam, Anupam Agarwal, Bharat B Aggarwal, Maria Agnello, Patrizia Agostinis, Javed N Agrewala, Alexander Agrotis, Patricia V Aguilar, S Tariq Ahmad, Zubair M Ahmed, Ulises Ahumada-Castro, Sonja Aits, Shu Aizawa, Yunus Akkoc, Tonia Akoumianaki, Hafize Aysin Akpinar, Ahmed M Al-Abd, Lina Al-Akra, Abeer Al-Gharaibeh, Moulay A Alaoui-Jamali, Simon Alberti, Elísabet Alcocer-Gómez, Cristiano Alessandri, Muhammad Ali, M Abdul Alim Al-Bari, Saeb Aliwaini, Javad Alizadeh, Eugènia Almacellas, Alexandru Almasan, Alicia Alonso, Guillermo D Alonso, Nihal Altan-Bonnet, Dario C Altieri, Élida M C Álvarez, Sara Alves, Cristine Alves da Costa, Mazen M Alzaharna, Marialaura Amadio, Consuelo Amantini, Cristina Amaral, Susanna Ambrosio, Amal O Amer, Veena Ammanathan, Zhenyi An, Stig U Andersen, Shaida A Andrabi, Magaiver Andrade-Silva, Allen M Andres, Sabrina Angelini, David Ann, Uche C Anozie, Mohammad Y Ansari, Pedro Antas, Adam Antebi, Zuriñe Antón, Tahira Anwar, Lionel Apetoh, Nadezda Apostolova, Toshiyuki Araki, Yasuhiro Araki, Kohei Arasaki, Wagner L Araújo, Jun Araya, Catherine Arden, Maria-Angeles Arévalo, Sandro Arguelles, Esperanza Arias, Jyothi Arikkath, Hirokazu Arimoto, Aileen R Ariosa, Darius Armstrong-James, Laetitia Arnauné-Pelloquin, Angeles Aroca, Daniela S Arroyo, Ivica Arsov, Rubén Artero, Dalia Maria Lucia Asaro, Michael Aschner, Milad Ashrafizadeh, Osnat Ashur-Fabian, Atanas G Atanasov, Alicia K Au, Patrick Auberger, Holger W Auner, Laure Aurelian, Riccardo Autelli, Laura Avagliano, Yenniffer Ávalos, Sanja Aveic, Célia Alexandra Aveleira, Tamar Avin-Wittenberg, Yucel Aydin, Scott Ayton, Srinivas Ayyadevara, Maria Azzopardi, Misuzu Baba, Jonathan M Backer, Steven K Backues, Dong-Hun Bae, Ok-Nam Bae, Soo Han Bae, Eric H Baehrecke, Ahruem Baek, Seung-Hoon Baek, Sung Hee Baek, Giacinto Bagetta, Agnieszka Bagniewska-Zadworna, Hua Bai, Jie Bai, Xiyuan Bai, Yidong Bai, Nandadulal Bairagi, Shounak Baksi, Teresa Balbi, Cosima T Baldari, Walter Balduini, Andrea Ballabio, Maria Ballester, Salma Balazadeh, Rena Balzan, Rina Bandopadhyay, Sreeparna Banerjee, Sulagna Banerjee, Ágnes Bánréti, Yan Bao, Mauricio S Baptista, Alessandra Baracca, Cristiana Barbati, Ariadna Bargiela, Daniela Barilà, Peter G Barlow, Sami J Barmada, Esther Barreiro, George E Barreto, Jiri Bartek, Bonnie Bartel, Alberto Bartolome, Gaurav R Barve, Suresh H Basagoudanavar, Diane C Bassham, Robert C Bast Jr, Alakananda Basu, Henri Batoko, Isabella Batten, Etienne E Baulieu, Bradley L Baumgarner, Jagadeesh Bayry, Rupert Beale, Isabelle Beau, Florian Beaumatin, Luiz R G Bechara, George R Beck Jr, Michael F Beers, Jakob Begun, Christian Behrends, Georg M N Behrens, Roberto Bei, Eloy Bejarano, Shai Bel, Christian Behl, Amine Belaid, Naïma Belgareh-Touzé, Cristina Bellarosa, Francesca Belleudi, Melissa Belló Pérez, Raquel Bello-Morales, Jackeline Soares de Oliveira Beltran, Sebastián Beltran, Doris Mangiaracina Benbrook, Mykolas Bendorius, Bruno A Benitez, Irene Benito-Cuesta, Julien Bensalem, Martin W Berchtold, Sabina Berezowska, Daniele Bergamaschi, Matteo Bergami, Andreas Bergmann, Laura Berliocchi, Clarisse Berlioz-Torrent, Amélie Bernard, Lionel Berthoux, Cagri G Besirli, Sebastien Besteiro, Virginie M Betin, Rudi Beyaert, Jelena S Bezbradica, Kiran Bhaskar, Ingrid Bhatia-Kissova, Resham Bhattacharya, Sujoy Bhattacharya, Shalmoli Bhattacharyya, Md Shenuarin Bhuiyan, Sujit Kumar Bhutia, Lanrong Bi, Xiaolin Bi, Trevor J Biden, Krikor Bijian, Viktor A Billes, Nadine Binart, Claudia Bincoletto, Asa B Birgisdottir, Geir Bjorkoy, Gonzalo Blanco, Ana Blas-Garcia, Janusz Blasiak, Robert Blomgran, Klas Blomgren, Janice S Blum, Emilio Boada-Romero, Mirta Boban, Kathleen Boesze-Battaglia, Philippe Boeuf, Barry Boland, Pascale Bomont, Paolo Bonaldo, Srinivasa Reddy Bonam, Laura Bonfili, Juan S Bonifacino, Brian A Boone, Martin D Bootman, Matteo Bordi, Christoph Borner, Beat C Bornhauser, Gautam Borthakur, Jürgen Bosch, Santanu Bose, Luis M Botana, Juan Botas, Chantal M Boulanger, Michael E Boulton, Mathieu Bourdenx, Benjamin Bourgeois, Nollaig M Bourke, Guilhem Bousquet, Patricia Boya, Peter V Bozhkov, Luiz H M Bozi, Tolga O Bozkurt, Doug E Brackney, Christian H Brandts, Ralf J Braun, Gerhard H Braus, Roberto Bravo-Sagua, José M Bravo-San Pedro, Patrick Brest, Marie-Agnès Bringer, Alfredo Briones-Herrera, V Courtney Broaddus, Peter Brodersen, Jeffrey L Brodsky, Steven L Brody, Paola G Bronson, Jeff M Bronstein, Carolyn N Brown, Rhoderick E Brown, Patricia C Brum, John H Brumell, Nicola Brunetti-Pierri, Daniele Bruno, Robert J Bryson-Richardson, Cecilia Bucci, Carmen Buchrieser, Marta Bueno, Laura Elisa Buitrago-Molina, Simone Buraschi, Shilpa Buch, J Ross Buchan, Erin M Buckingham, Hikmet Budak, Mauricio Budini, Geert Bultynck, Florin Burada, Joseph R Burgoyne, M Isabel Burón, Victor Bustos, Sabrina Büttner, Elena Butturini, Aaron Byrd, Isabel Cabas, Sandra Cabrera-Benitez, Ken Cadwell, Jingjing Cai, Lu Cai, Qian Cai, Montserrat Cairó, Jose A Calbet, Guy A Caldwell, Kim A Caldwell, Jarrod A Call, Riccardo Calvani, Ana C Calvo, Miguel Calvo-Rubio Barrera, Niels Os Camara, Jacques H Camonis, Nadine Camougrand, Michelangelo Campanella, Edward M Campbell, François-Xavier Campbell-Valois, Silvia Campello, Ilaria Campesi, Juliane C Campos, Olivier Camuzard, Jorge Cancino, Danilo Candido de Almeida, Laura Canesi, Isabella Caniggia, Barbara Canonico, Carles Cantí, Bin Cao, Michele Caraglia, Beatriz Caramés, Evie H Carchman, Elena Cardenal-Muñoz, Cesar Cardenas, Luis Cardenas, Sandra M Cardoso, Jennifer S Carew, Georges F Carle, Gillian Carleton, Silvia Carloni, Didac Carmona-Gutierrez, Leticia A Carneiro, Oliana Carnevali, Julian M Carosi, Serena Carra, Alice Carrier, Lucie Carrier, Bernadette Carroll, A Brent Carter, Andreia Neves Carvalho, Magali Casanova, Caty Casas, Josefina Casas, Chiara Cassioli, Eliseo F Castillo, Karen Castillo, Sonia Castillo-Lluva, Francesca Castoldi, Marco Castori, Ariel F Castro, Margarida Castro-Caldas, Javier Castro-Hernandez, Susana Castro-Obregon, Sergio D Catz, Claudia Cavadas, Federica Cavaliere, Gabriella Cavallini, Maria Cavinato, Maria L Cayuela, Paula Cebollada Rica, Valentina Cecarini, Francesco Cecconi, Marzanna Cechowska-Pasko, Simone Cenci, Victòria Ceperuelo-Mallafré, João J Cerqueira, Janete M Cerutti, Davide Cervia, Vildan Bozok Cetintas, Silvia Cetrullo, Han-Jung Chae, Andrei S Chagin, Chee-Yin Chai, Gopal Chakrabarti, Oishee Chakrabarti, Tapas Chakraborty, Trinad Chakraborty, Mounia Chami, Georgios Chamilos, David W Chan, Edmond Y W Chan, Edward D Chan, H Y Edwin Chan, Helen H Chan, Hung Chan, Matthew T V Chan, Yau Sang Chan, Partha K Chandra, Chih-Peng Chang, Chunmei Chang, Hao-Chun Chang, Kai Chang, Jie Chao, Tracey Chapman, Nicolas Charlet-Berguerand, Samrat Chatterjee, Shail K Chaube, Anu Chaudhary, Santosh Chauhan, Edward Chaum, Frédéric Checler, Michael E Cheetham, Chang-Shi Chen, Guang-Chao Chen, Jian-Fu Chen, Liam L Chen, Leilei Chen, Lin Chen, Mingliang Chen, Mu-Kuan Chen, Ning Chen, Quan Chen, Ruey-Hwa Chen, Shi Chen, Wei Chen, Weiqiang Chen, Xin-Ming Chen, Xiong-Wen Chen, Xu Chen, Yan Chen, Ye-Guang Chen, Yingyu Chen, Yongqiang Chen, Yu-Jen Chen, Yue-Qin Chen, Zhefan Stephen Chen, Zhi Chen, Zhi-Hua Chen, Zhijian J Chen, Zhixiang Chen, Hanhua Cheng, Jun Cheng, Shi-Yuan Cheng, Wei Cheng, Xiaodong Cheng, Xiu-Tang Cheng, Yiyun Cheng, Zhiyong Cheng, Zhong Chen, Heesun Cheong, Jit Kong Cheong, Boris V Chernyak, Sara Cherry, Chi Fai Randy Cheung, Chun Hei Antonio Cheung, King-Ho Cheung, Eric Chevet, Richard J Chi, Alan Kwok Shing Chiang, Ferdinando Chiaradonna, Roberto Chiarelli, Mario Chiariello, Nathalia Chica, Susanna Chiocca, Mario Chiong, Shih-Hwa Chiou, Abhilash I Chiramel, Valerio Chiurchiù, Dong-Hyung Cho, Seong-Kyu Choe, Augustine M K Choi, Mary E Choi, Kamalika Roy Choudhury, Norman S Chow, Charleen T Chu, Jason P Chua, John Jia En Chua, Hyewon Chung, Kin Pan Chung, Seockhoon Chung, So-Hyang Chung, Yuen-Li Chung, Valentina Cianfanelli, Iwona A Ciechomska, Mariana Cifuentes, Laura Cinque, Sebahattin Cirak, Mara Cirone, Michael J Clague, Robert Clarke, Emilio Clementi, Eliana M Coccia, Patrice Codogno, Ehud Cohen, Mickael M Cohen, Tania Colasanti, Fiorella Colasuonno, Robert A Colbert, Anna Colell, Miodrag Čolić, Nuria S Coll, Mark O Collins, María I Colombo, Daniel A Colón-Ramos, Lydie Combaret, Sergio Comincini, Márcia R Cominetti, Antonella Consiglio, Andrea Conte, Fabrizio Conti, Viorica Raluca Contu, Mark R Cookson, Kevin M Coombs, Isabelle Coppens, Maria Tiziana Corasaniti, Dale P Corkery, Nils Cordes, Katia Cortese, Maria do Carmo Costa, Sarah Costantino, Paola Costelli, Ana Coto-Montes, Peter J Crack, Jose L Crespo, Alfredo Criollo, Valeria Crippa, Riccardo Cristofani, Tamas Csizmadia, Antonio Cuadrado, Bing Cui, Jun Cui, Yixian Cui, Yong Cui, Emmanuel Culetto, Andrea C Cumino, Andrey V Cybulsky, Mark J Czaja, Stanislaw J Czuczwar, Stefania D'Adamo, Marcello D'Amelio, Daniela D'Arcangelo, Andrew C D'Lugos, Gabriella D'Orazi, James A da Silva, Hormos Salimi Dafsari, Ruben K Dagda, Yasin Dagdas, Maria Daglia, Xiaoxia Dai, Yun Dai, Yuyuan Dai, Jessica Dal Col, Paul Dalhaimer, Luisa Dalla Valle, Tobias Dallenga, Guillaume Dalmasso, Markus Damme, Ilaria Dando, Nico P Dantuma, April L Darling, Hiranmoy Das, Srinivasan Dasarathy, Santosh K Dasari, Srikanta Dash, Oliver Daumke, Adrian N Dauphinee, Jeffrey S Davies, Valeria A Dávila, Roger J Davis, Tanja Davis, Sharadha Dayalan Naidu, Francesca De Amicis, Karolien De Bosscher, Francesca De Felice, Lucia De Franceschi, Chiara De Leonibus, Mayara G de Mattos Barbosa, Guido R Y De Meyer, Angelo De Milito, Cosimo De Nunzio, Clara De Palma, Mauro De Santi, Claudio De Virgilio, Daniela De Zio, Jayanta Debnath, Brian J DeBosch, Jean-Paul Decuypere, Mark A Deehan, Gianluca Deflorian, James DeGregori, Benjamin Dehay, Gabriel Del Rio, Joe R Delaney, Lea M D Delbridge, Elizabeth Delorme-Axford, M Victoria Delpino, Francesca Demarchi, Vilma Dembitz, Nicholas D Demers, Hongbin Deng, Zhiqiang Deng, Joern Dengjel, Paul Dent, Donna Denton, Melvin L DePamphilis, Channing J Der, Vojo Deretic, Albert Descoteaux, Laura Devis, Sushil Devkota, Olivier Devuyst, Grant Dewson, Mahendiran Dharmasivam, Rohan Dhiman, Diego di Bernardo, Manlio Di Cristina, Fabio Di Domenico, Pietro Di Fazio, Alessio Di Fonzo, Giovanni Di Guardo, Gianni M Di Guglielmo, Luca Di Leo, Chiara Di Malta, Alessia Di Nardo, Martina Di Rienzo, Federica Di Sano, George Diallinas, Jiajie Diao, Guillermo Diaz-Araya, Inés Díaz-Laviada, Jared M Dickinson, Marc Diederich, Mélanie Dieudé, Ivan Dikic, Shiping Ding, Wen-Xing Ding, Luciana Dini, Jelena Dinić, Miroslav Dinic, Albena T Dinkova-Kostova, Marc S Dionne, Jörg H W Distler, Abhinav Diwan, Ian M C Dixon, Mojgan Djavaheri-Mergny, Ina Dobrinski, Oxana Dobrovinskaya, Radek Dobrowolski, Renwick C J Dobson, Jelena Đokić, Serap Dokmeci Emre, Massimo Donadelli, Bo Dong, Xiaonan Dong, Zhiwu Dong, Gerald W Dorn Ii, Volker Dotsch, Huan Dou, Juan Dou, Moataz Dowaidar, Sami Dridi, Liat Drucker, Ailian Du, Caigan Du, Guangwei Du, Hai-Ning Du, Li-Lin Du, André du Toit, Shao-Bin Duan, Xiaoqiong Duan, Sónia P Duarte, Anna Dubrovska, Elaine A Dunlop, Nicolas Dupont, Raúl V Durán, Bilikere S Dwarakanath, Sergey A Dyshlovoy, Darius Ebrahimi-Fakhari, Leopold Eckhart, Charles L Edelstein, Thomas Efferth, Eftekhar Eftekharpour, Ludwig Eichinger, Nabil Eid, Tobias Eisenberg, N Tony Eissa, Sanaa Eissa, Miriam Ejarque, Abdeljabar El Andaloussi, Nazira El-Hage, Shahenda El-Naggar, Anna Maria Eleuteri, Eman S El-Shafey, Mohamed Elgendy, Aristides G Eliopoulos, María M Elizalde, Philip M Elks, Hans-Peter Elsasser, Eslam S Elsherbiny, Brooke M Emerling, N C Tolga Emre, Christina H Eng, Nikolai Engedal, Anna-Mart Engelbrecht, Agnete S T Engelsen, Jorrit M Enserink, Ricardo Escalante, Audrey Esclatine, Mafalda Escobar-Henriques, Eeva-Liisa Eskelinen, Lucile Espert, Makandjou-Ola Eusebio, Gemma Fabrias, Cinzia Fabrizi, Antonio Facchiano, Francesco Facchiano, Bengt Fadeel, Claudio Fader, Alex C Faesen, W Douglas Fairlie, Alberto Falcó, Bjorn H Falkenburger, Daping Fan, Jie Fan, Yanbo Fan, Evandro F Fang, Yanshan Fang, Yognqi Fang, Manolis Fanto, Tamar Farfel-Becker, Mathias Faure, Gholamreza Fazeli, Anthony O Fedele, Arthur M Feldman, Du Feng, Jiachun Feng, Lifeng Feng, Yibin Feng, Yuchen Feng, Wei Feng, Thais Fenz Araujo, Thomas A Ferguson, Álvaro F Fernández, Jose C Fernandez-Checa, Sonia Fernández-Veledo, Alisdair R Fernie, Anthony W Ferrante Jr, Alessandra Ferraresi, Merari F Ferrari, Julio C B Ferreira, Susan Ferro-Novick, Antonio Figueras, Riccardo Filadi, Nicoletta Filigheddu, Eduardo Filippi-Chiela, Giuseppe Filomeni, Gian Maria Fimia, Vittorio Fineschi, Francesca Finetti, Steven Finkbeiner, Edward A Fisher, Paul B Fisher, Flavio Flamigni, Steven J Fliesler, Trude H Flo, Ida Florance, Oliver Florey, Tullio Florio, Erika Fodor, Carlo Follo, Edward A Fon, Antonella Forlino, Francesco Fornai, Paola Fortini, Anna Fracassi, Alessandro Fraldi, Brunella Franco, Rodrigo Franco, Flavia Franconi, Lisa B Frankel, Scott L Friedman, Leopold F Fröhlich, Gema Frühbeck, Jose M Fuentes, Yukio Fujiki, Naonobu Fujita, Yuuki Fujiwara, Mitsunori Fukuda, Simone Fulda, Luc Furic, Norihiko Furuya, Carmela Fusco, Michaela U Gack, Lidia Gaffke, Sehamuddin Galadari, Alessia Galasso, Maria F Galindo, Sachith Gallolu Kankanamalage, Lorenzo Galluzzi, Vincent Galy, Noor Gammoh, Boyi Gan, Ian G Ganley, Feng Gao, Hui Gao, Minghui Gao, Ping Gao, Shou-Jiang Gao, Wentao Gao, Xiaobo Gao, Ana Garcera, Maria Noé Garcia, Verónica E Garcia, Francisco García-Del Portillo, Vega Garcia-Escudero, Aracely Garcia-Garcia, Marina Garcia-Macia, Diana García-Moreno, Carmen Garcia-Ruiz, Patricia García-Sanz, Abhishek D Garg, Ricardo Gargini, Tina Garofalo, Robert F Garry, Nils C Gassen, Damian Gatica, Liang Ge, Wanzhong Ge, Ruth Geiss-Friedlander, Cecilia Gelfi, Pascal Genschik, Ian E Gentle, Valeria Gerbino, Christoph Gerhardt, Kyla Germain, Marc Germain, David A Gewirtz, Elham Ghasemipour Afshar, Saeid Ghavami, Alessandra Ghigo, Manosij Ghosh, Georgios Giamas, Claudia Giampietri, Alexandra Giatromanolaki, Gary E Gibson, Spencer B Gibson, Vanessa Ginet, Edward Giniger, Carlotta Giorgi, Henrique Girao, Stephen E Girardin, Mridhula Giridharan, Sandy Giuliano, Cecilia Giulivi, Sylvie Giuriato, Julien Giustiniani, Alexander Gluschko, Veit Goder, Alexander Goginashvili, Jakub Golab, David C Goldstone, Anna Golebiewska, Luciana R Gomes, Rodrigo Gomez, Rubén Gómez-Sánchez, Maria Catalina Gomez-Puerto, Raquel Gomez-Sintes, Qingqiu Gong, Felix M Goni, Javier González-Gallego, Tomas Gonzalez-Hernandez, Rosa A Gonzalez-Polo, Jose A Gonzalez-Reyes, Patricia González-Rodríguez, Ing Swie Goping, Marina S Gorbatyuk, Nikolai V Gorbunov, Kıvanç Görgülü, Roxana M Gorojod, Sharon M Gorski, Sandro Goruppi, Cecilia Gotor, Roberta A Gottlieb, Illana Gozes, Devrim Gozuacik, Martin Graef, Markus H Gräler, Veronica Granatiero, Daniel Grasso, Joshua P Gray, Douglas R Green, Alexander Greenhough, Stephen L Gregory, Edward F Griffin, Mark W Grinstaff, Frederic Gros, Charles Grose, Angelina S Gross, Florian Gruber, Paolo Grumati, Tilman Grune, Xueyan Gu, Jun-Lin Guan, Carlos M Guardia, Kishore Guda, Flora Guerra, Consuelo Guerri, Prasun Guha, Carlos Guillén, Shashi Gujar, Anna Gukovskaya, Ilya Gukovsky, Jan Gunst, Andreas Günther, Anyonya R Guntur, Chuanyong Guo, Chun Guo, Hongqing Guo, Lian-Wang Guo, Ming Guo, Pawan Gupta, Shashi Kumar Gupta, Swapnil Gupta, Veer Bala Gupta, Vivek Gupta, Asa B Gustafsson, David D Gutterman, Ranjitha H B, Annakaisa Haapasalo, James E Haber, Aleksandra Hać, Shinji Hadano, 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Sriganesh Ramachandra Rao, Abdelhaq Rami, Ignacio Ramírez-Pardo, David B Ramsden, Felix Randow, Pundi N Rangarajan, Danilo Ranieri, Hai Rao, Lang Rao, Rekha Rao, Sumit Rathore, J Arjuna Ratnayaka, Edward A Ratovitski, Palaniyandi Ravanan, Gloria Ravegnini, Swapan K Ray, Babak Razani, Vito Rebecca, Fulvio Reggiori, Anne Régnier-Vigouroux, Andreas S Reichert, David Reigada, Jan H Reiling, Theo Rein, Siegfried Reipert, Rokeya Sultana Rekha, Hongmei Ren, Jun Ren, Weichao Ren, Tristan Renault, Giorgia Renga, Karen Reue, Kim Rewitz, Bruna Ribeiro de Andrade Ramos, S Amer Riazuddin, Teresa M Ribeiro-Rodrigues, Jean-Ehrland Ricci, Romeo Ricci, Victoria Riccio, Des R Richardson, Yasuko Rikihisa, Makarand V Risbud, Ruth M Risueño, Konstantinos Ritis, Salvatore Rizza, Rosario Rizzuto, Helen C Roberts, Luke D Roberts, Katherine J Robinson, Maria Carmela Roccheri, Stephane Rocchi, George G Rodney, Tiago Rodrigues, Vagner Ramon Rodrigues Silva, Amaia Rodriguez, Ruth Rodriguez-Barrueco, Nieves Rodriguez-Henche, Humberto Rodriguez-Rocha, Jeroen Roelofs, Robert S Rogers, Vladimir V Rogov, Ana I Rojo, Krzysztof Rolka, Vanina Romanello, Luigina Romani, Alessandra Romano, Patricia S Romano, David Romeo-Guitart, Luis C Romero, Montserrat Romero, Joseph C Roney, Christopher Rongo, Sante Roperto, Mathias T Rosenfeldt, Philip Rosenstiel, Anne G Rosenwald, Kevin A Roth, Lynn Roth, Steven Roth, Kasper M A Rouschop, Benoit D Roussel, Sophie Roux, Patrizia Rovere-Querini, Ajit Roy, Aurore Rozieres, Diego Ruano, David C Rubinsztein, Maria P Rubtsova, Klaus Ruckdeschel, Christoph Ruckenstuhl, Emil Rudolf, Rüdiger Rudolf, Alessandra Ruggieri, Avnika Ashok Ruparelia, Paola Rusmini, Ryan R Russell, Gian Luigi Russo, Maria Russo, Rossella Russo, Oxana O Ryabaya, Kevin M Ryan, Kwon-Yul Ryu, Maria Sabater-Arcis, Ulka Sachdev, Michael Sacher, Carsten Sachse, Abhishek Sadhu, Junichi Sadoshima, Nathaniel Safren, Paul Saftig, Antonia P Sagona, Gaurav Sahay, Amirhossein Sahebkar, Mustafa Sahin, Ozgur Sahin, Sumit Sahni, Nayuta Saito, Shigeru Saito, Tsunenori Saito, Ryohei Sakai, Yasuyoshi Sakai, Jun-Ichi Sakamaki, Kalle Saksela, Gloria Salazar, Anna Salazar-Degracia, Ghasem H Salekdeh, Ashok K Saluja, Belém Sampaio-Marques, Maria Cecilia Sanchez, Jose A Sanchez-Alcazar, Victoria Sanchez-Vera, Vanessa Sancho-Shimizu, J Thomas Sanderson, Marco Sandri, Stefano Santaguida, Laura Santambrogio, Magda M Santana, Giorgio Santoni, Alberto Sanz, Pascual Sanz, Shweta Saran, Marco Sardiello, Timothy J Sargeant, Apurva Sarin, Chinmoy Sarkar, Sovan Sarkar, Maria-Rosa Sarrias, Surajit Sarkar, Dipanka Tanu Sarmah, Jaakko Sarparanta, Aishwarya Sathyanarayan, Ranganayaki Sathyanarayanan, K Matthew Scaglione, Francesca Scatozza, Liliana Schaefer, Zachary T Schafer, Ulrich E Schaible, Anthony H V Schapira, Michael Scharl, Hermann M Schatzl, Catherine H Schein, Wiep Scheper, David Scheuring, Maria Vittoria Schiaffino, Monica Schiappacassi, Rainer Schindl, Uwe Schlattner, Oliver Schmidt, Roland Schmitt, Stephen D Schmidt, Ingo Schmitz, Eran Schmukler, Anja Schneider, Bianca E Schneider, Romana Schober, Alejandra C Schoijet, Micah B Schott, Michael Schramm, Bernd Schröder, Kai Schuh, Christoph Schüller, Ryan J Schulze, Lea Schürmanns, Jens C Schwamborn, Melanie Schwarten, Filippo Scialo, Sebastiano Sciarretta, Melanie J Scott, Kathleen W Scotto, A Ivana Scovassi, Andrea Scrima, Aurora Scrivo, David Sebastian, Salwa Sebti, Simon Sedej, Laura Segatori, Nava Segev, Per O Seglen, Iban Seiliez, Ekihiro Seki, Scott B Selleck, Frank W Sellke, Joshua T Selsby, Michael Sendtner, Serif Senturk, Elena Seranova, Consolato Sergi, Ruth Serra-Moreno, Hiromi Sesaki, Carmine Settembre, Subba Rao Gangi Setty, Gianluca Sgarbi, Ou Sha, John J Shacka, Javeed A Shah, Dantong Shang, Changshun Shao, Feng Shao, Soroush Sharbati, Lisa M Sharkey, Dipali Sharma, Gaurav Sharma, Kulbhushan Sharma, Pawan Sharma, Surendra Sharma, Han-Ming Shen, Hongtao Shen, Jiangang Shen, Ming Shen, Weili Shen, Zheni Shen, Rui 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Sok, Giancarlo Solaini, Thierry Soldati, Scott A Soleimanpour, Rosa M Soler, Alexei Solovchenko, Jason A Somarelli, Avinash Sonawane, Fuyong Song, Hyun Kyu Song, Ju-Xian Song, Kunhua Song, Zhiyin Song, Leandro R Soria, Maurizio Sorice, Alexander A Soukas, Sandra-Fausia Soukup, Diana Sousa, Nadia Sousa, Paul A Spagnuolo, Stephen A Spector, M M Srinivas Bharath, Daret St Clair, Venturina Stagni, Leopoldo Staiano, Clint A Stalnecker, Metodi V Stankov, Peter B Stathopulos, Katja Stefan, Sven Marcel Stefan, Leonidas Stefanis, Joan S Steffan, Alexander Steinkasserer, Harald Stenmark, Jared Sterneckert, Craig Stevens, Veronika Stoka, Stephan Storch, Björn Stork, Flavie Strappazzon, Anne Marie Strohecker, Dwayne G Stupack, Huanxing Su, Ling-Yan Su, Longxiang Su, Ana M Suarez-Fontes, Carlos S Subauste, Selvakumar Subbian, Paula V Subirada, Ganapasam Sudhandiran, Carolyn M Sue, Xinbing Sui, Corey Summers, Guangchao Sun, Jun Sun, Kang Sun, Meng-Xiang Sun, Qiming Sun, Yi Sun, Zhongjie Sun, Karen K S Sunahara, Eva Sundberg, Katalin Susztak, Peter Sutovsky, Hidekazu Suzuki, Gary Sweeney, J David Symons, Stephen Cho Wing Sze, Nathaniel J Szewczyk, Anna Tabęcka-Łonczynska, Claudio Tabolacci, Frank Tacke, Heinrich Taegtmeyer, Marco Tafani, Mitsuo Tagaya, Haoran Tai, Stephen W G Tait, Yoshinori Takahashi, Szabolcs Takats, Priti Talwar, Chit Tam, Shing Yau Tam, Davide Tampellini, Atsushi Tamura, Chong Teik Tan, Eng-King Tan, Ya-Qin Tan, Masaki Tanaka, Motomasa Tanaka, Daolin Tang, Jingfeng Tang, Tie-Shan Tang, Isei Tanida, Zhipeng Tao, Mohammed Taouis, Lars Tatenhorst, Nektarios Tavernarakis, Allen Taylor, Gregory A Taylor, Joan M Taylor, Elena Tchetina, Andrew R Tee, Irmgard Tegeder, David Teis, Natercia Teixeira, Fatima Teixeira-Clerc, Kumsal A Tekirdag, Tewin Tencomnao, Sandra Tenreiro, Alexei V Tepikin, Pilar S Testillano, Gianluca Tettamanti, Pierre-Louis Tharaux, Kathrin Thedieck, Arvind A Thekkinghat, Stefano Thellung, Josephine W Thinwa, V P Thirumalaikumar, Sufi Mary Thomas, Paul G Thomes, Andrew Thorburn, Lipi Thukral, Thomas Thum, Michael Thumm, Ling Tian, Ales Tichy, Andreas Till, Vincent Timmerman, Vladimir I Titorenko, Sokol V Todi, Krassimira Todorova, Janne M Toivonen, Luana Tomaipitinca, Dhanendra Tomar, Cristina Tomas-Zapico, Sergej Tomić, Benjamin Chun-Kit Tong, Chao Tong, Xin Tong, Sharon A Tooze, Maria L Torgersen, Satoru Torii, Liliana Torres-López, Alicia Torriglia, Christina G Towers, Roberto Towns, Shinya Toyokuni, Vladimir Trajkovic, Donatella Tramontano, Quynh-Giao Tran, Leonardo H Travassos, Charles B Trelford, Shirley Tremel, Ioannis P Trougakos, Betty P Tsao, Mario P Tschan, Hung-Fat Tse, Tak Fu Tse, Hitoshi Tsugawa, Andrey S Tsvetkov, David A Tumbarello, Yasin Tumtas, María J Tuñón, Sandra Turcotte, Boris Turk, Vito Turk, Bradley J Turner, Richard I Tuxworth, Jessica K Tyler, Elena V Tyutereva, Yasuo Uchiyama, Aslihan Ugun-Klusek, Holm H Uhlig, Marzena Ułamek-Kozioł, Ilya V Ulasov, Midori Umekawa, Christian Ungermann, Rei Unno, Sylvie Urbe, Elisabet Uribe-Carretero, Suayib Üstün, Vladimir N Uversky, Thomas Vaccari, Maria I Vaccaro, Björn F Vahsen, Helin Vakifahmetoglu-Norberg, Rut Valdor, Maria J Valente, Ayelén Valko, Richard B Vallee, Angela M Valverde, Greet Van den Berghe, Stijn van der Veen, Luc Van Kaer, Jorg van Loosdregt, Sjoerd J L van Wijk, Wim Vandenberghe, Ilse Vanhorebeek, Marcos A Vannier-Santos, Nicola Vannini, M Cristina Vanrell, Chiara Vantaggiato, Gabriele Varano, Isabel Varela-Nieto, Máté Varga, M Helena Vasconcelos, Somya Vats, Demetrios G Vavvas, Ignacio Vega-Naredo, Silvia Vega-Rubin-de-Celis, Guillermo Velasco, Ariadna P Velázquez, Tibor Vellai, Edo Vellenga, Francesca Velotti, Mireille Verdier, Panayotis Verginis, Isabelle Vergne, Paul Verkade, Manish Verma, Patrik Verstreken, Tim Vervliet, Jörg Vervoorts, Alexandre T Vessoni, Victor M Victor, Michel Vidal, Chiara Vidoni, Otilia V Vieira, Richard D Vierstra, Sonia Viganó, Helena Vihinen, Vinoy Vijayan, Miquel Vila, Marçal Vilar, José M Villalba, Antonio Villalobo, Beatriz Villarejo-Zori, Francesc Villarroya, Joan Villarroya, Olivier Vincent, Cecile Vindis, Christophe Viret, Maria Teresa Viscomi, Dora Visnjic, Ilio Vitale, David J Vocadlo, Olga V Voitsekhovskaja, Cinzia Volonté, Mattia Volta, Marta Vomero, Clarissa Von Haefen, Marc A Vooijs, Wolfgang Voos, Ljubica Vucicevic, Richard Wade-Martins, Satoshi Waguri, Kenrick A Waite, Shuji Wakatsuki, David W Walker, Mark J Walker, Simon A Walker, Jochen Walter, Francisco G Wandosell, Bo Wang, Chao-Yung Wang, Chen Wang, Chenran Wang, Chenwei Wang, Cun-Yu Wang, Dong Wang, Fangyang Wang, Feng Wang, Fengming Wang, Guansong Wang, Han Wang, Hao Wang, Hexiang Wang, Hong-Gang Wang, Jianrong Wang, Jigang Wang, Jiou Wang, Jundong Wang, Kui Wang, Lianrong Wang, Liming Wang, Maggie Haitian Wang, Meiqing Wang, Nanbu Wang, Pengwei Wang, Peipei Wang, Ping Wang, Ping Wang, Qing Jun Wang, Qing Wang, Qing Kenneth Wang, Qiong A Wang, Wen-Tao Wang, Wuyang Wang, Xinnan Wang, Xuejun Wang, Yan Wang, Yanchang Wang, Yanzhuang Wang, Yen-Yun Wang, Yihua Wang, Yipeng Wang, Yu Wang, Yuqi Wang, Zhe Wang, Zhenyu Wang, Zhouguang Wang, Gary Warnes, Verena Warnsmann, Hirotaka Watada, Eizo Watanabe, Maxinne Watchon, Anna Wawrzyńska, Timothy E Weaver, Grzegorz Wegrzyn, Ann M Wehman, Huafeng Wei, Lei Wei, Taotao Wei, Yongjie Wei, Oliver H Weiergräber, Conrad C Weihl, Günther Weindl, Ralf Weiskirchen, Alan Wells, Runxia H Wen, Xin Wen, Antonia Werner, Beatrice Weykopf, Sally P Wheatley, J Lindsay Whitton, Alexander J Whitworth, Katarzyna Wiktorska, Manon E Wildenberg, Tom Wileman, Simon Wilkinson, Dieter Willbold, Brett Williams, Robin S B Williams, Roger L Williams, Peter R Williamson, Richard A Wilson, Beate Winner, Nathaniel J Winsor, Steven S Witkin, Harald Wodrich, Ute Woehlbier, Thomas Wollert, Esther Wong, Jack Ho Wong, Richard W Wong, Vincent Kam Wai Wong, W Wei-Lynn Wong, An-Guo Wu, Chengbiao Wu, Jian Wu, Junfang Wu, Kenneth K Wu, Min Wu, Shan-Ying Wu, Shengzhou Wu, Shu-Yan Wu, Shufang Wu, William K K Wu, Xiaohong Wu, Xiaoqing Wu, Yao-Wen Wu, Yihua Wu, Ramnik J Xavier, Hongguang Xia, Lixin Xia, Zhengyuan Xia, Ge Xiang, Jin Xiang, Mingliang Xiang, Wei Xiang, Bin Xiao, Guozhi Xiao, Hengyi Xiao, Hong-Tao Xiao, Jian Xiao, Lan Xiao, Shi Xiao, Yin Xiao, Baoming Xie, Chuan-Ming Xie, Min Xie, Yuxiang Xie, Zhiping Xie, Zhonglin Xie, Maria Xilouri, Congfeng Xu, En Xu, Haoxing Xu, Jing Xu, JinRong Xu, Liang Xu, Wen Wen Xu, Xiulong Xu, Yu Xue, Sokhna M S Yakhine-Diop, Masamitsu Yamaguchi, Osamu Yamaguchi, Ai Yamamoto, Shunhei Yamashina, Shengmin Yan, Shian-Jang Yan, Zhen Yan, Yasuo Yanagi, Chuanbin Yang, Dun-Sheng Yang, Huan Yang, Huang-Tian Yang, Hui Yang, Jin-Ming Yang, Jing Yang, Jingyu Yang, Ling Yang, Liu Yang, Ming Yang, Pei-Ming Yang, Qian Yang, Seungwon Yang, Shu Yang, Shun-Fa Yang, Wannian Yang, Wei Yuan Yang, Xiaoyong Yang, Xuesong Yang, Yi Yang, Ying Yang, Honghong Yao, Shenggen Yao, Xiaoqiang Yao, Yong-Gang Yao, Yong-Ming Yao, Takahiro Yasui, Meysam Yazdankhah, Paul M Yen, Cong Yi, Xiao-Ming Yin, Yanhai Yin, Zhangyuan Yin, Ziyi Yin, Meidan Ying, Zheng Ying, Calvin K Yip, Stephanie Pei Tung Yiu, Young H Yoo, Kiyotsugu Yoshida, Saori R Yoshii, Tamotsu Yoshimori, Bahman Yousefi, Boxuan Yu, Haiyang Yu, Jun Yu, Jun Yu, Li Yu, Ming-Lung Yu, Seong-Woon Yu, Victor C Yu, W Haung Yu, Zhengping Yu, Zhou Yu, Junying Yuan, Ling-Qing Yuan, Shilin Yuan, Shyng-Shiou F Yuan, Yanggang Yuan, Zengqiang Yuan, Jianbo Yue, Zhenyu Yue, Jeanho Yun, Raymond L Yung, David N Zacks, Gabriele Zaffagnini, Vanessa O Zambelli, Isabella Zanella, Qun S Zang, Sara Zanivan, Silvia Zappavigna, Pilar Zaragoza, Konstantinos S Zarbalis, Amir Zarebkohan, Amira Zarrouk, Scott O Zeitlin, Jialiu Zeng, Ju-Deng Zeng, Eva Žerovnik, Lixuan Zhan, Bin Zhang, Donna D Zhang, Hanlin Zhang, Hong Zhang, Hong Zhang, Honghe Zhang, Huafeng Zhang, Huaye Zhang, Hui Zhang, Hui-Ling Zhang, Jianbin Zhang, Jianhua Zhang, Jing-Pu Zhang, Kalin Y B Zhang, Leshuai W Zhang, Lin Zhang, Lisheng Zhang, Lu Zhang, Luoying Zhang, Menghuan Zhang, Peng Zhang, Sheng Zhang, Wei Zhang, Xiangnan Zhang, Xiao-Wei Zhang, Xiaolei Zhang, Xiaoyan Zhang, Xin Zhang, Xinxin Zhang, Xu Dong Zhang, Yang Zhang, Yanjin Zhang, Yi Zhang, Ying-Dong Zhang, Yingmei Zhang, Yuan-Yuan Zhang, Yuchen Zhang, Zhe Zhang, Zhengguang Zhang, Zhibing Zhang, Zhihai Zhang, Zhiyong Zhang, Zili Zhang, Haobin Zhao, Lei Zhao, Shuang Zhao, Tongbiao Zhao, Xiao-Fan Zhao, Ying Zhao, Yongchao Zhao, Yongliang Zhao, Yuting Zhao, Guoping Zheng, Kai Zheng, Ling Zheng, Shizhong Zheng, Xi-Long Zheng, Yi Zheng, Zu-Guo Zheng, Boris Zhivotovsky, Qing Zhong, Ao Zhou, Ben Zhou, Cefan Zhou, Gang Zhou, Hao Zhou, Hong Zhou, Hongbo Zhou, Jie Zhou, Jing Zhou, Jing Zhou, Jiyong Zhou, Kailiang Zhou, Rongjia Zhou, Xu-Jie Zhou, Yanshuang Zhou, Yinghong Zhou, Yubin Zhou, Zheng-Yu Zhou, Zhou Zhou, Binglin Zhu, Changlian Zhu, Guo-Qing Zhu, Haining Zhu, Hongxin Zhu, Hua Zhu, Wei-Guo Zhu, Yanping Zhu, Yushan Zhu, Haixia Zhuang, Xiaohong Zhuang, Katarzyna Zientara-Rytter, Christine M Zimmermann, Elena Ziviani, Teresa Zoladek, Wei-Xing Zong, Dmitry B Zorov, Antonio Zorzano, Weiping Zou, Zhen Zou, Zhengzhi Zou, Steven Zuryn, Werner Zwerschke, Beate Brand-Saberi, X Charlie Dong, Chandra Shekar Kenchappa, Zuguo Li, Yong Lin, Shigeru Oshima, Yueguang Rong, Judith C Sluimer, Christina L Stallings, Chun-Kit Tong

    Autophagy   17 ( 1 )   1 - 382   2021.1

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    In 2008, we published the first set of guidelines for standardizing research in autophagy. Since then, this topic has received increasing attention, and many scientists have entered the field. Our knowledge base and relevant new technologies have also been expanding. Thus, it is important to formulate on a regular basis updated guidelines for monitoring autophagy in different organisms. Despite numerous reviews, there continues to be confusion regarding acceptable methods to evaluate autophagy, especially in multicellular eukaryotes. Here, we present a set of guidelines for investigators to select and interpret methods to examine autophagy and related processes, and for reviewers to provide realistic and reasonable critiques of reports that are focused on these processes. These guidelines are not meant to be a dogmatic set of rules, because the appropriateness of any assay largely depends on the question being asked and the system being used. Moreover, no individual assay is perfect for every situation, calling for the use of multiple techniques to properly monitor autophagy in each experimental setting. Finally, several core components of the autophagy machinery have been implicated in distinct autophagic processes (canonical and noncanonical autophagy), implying that genetic approaches to block autophagy should rely on targeting two or more autophagy-related genes that ideally participate in distinct steps of the pathway. Along similar lines, because multiple proteins involved in autophagy also regulate other cellular pathways including apoptosis, not all of them can be used as a specific marker for bona fide autophagic responses. Here, we critically discuss current methods of assessing autophagy and the information they can, or cannot, provide. Our ultimate goal is to encourage intellectual and technical innovation in the field.

    DOI： 10.1080/15548627.2020.1797280

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    日本分子生物学会年会プログラム・要旨集(Web)   42nd   2019

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  • グルタミン飢餓によりオートリソソームの成熟が促進される現象の発見

    朽津芳彦, 本間悠太, 藤田尚信, 福田光則

    日本生化学会大会(Web)   91st   2018

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  • Rabによるオートファジー制御

    朽津芳彦, 藤田尚信, 福田光則

    実験医学増刊号「The オートファジー」   35 ( 15 )   58 - 65   2017.9

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    Language：Japanese   Publishing type：Article, review, commentary, editorial, etc. (scientific journal)  

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    藤田尚信, 朽津芳彦, AMY Kiger, 福田光則

    日本細胞生物学会大会(Web)   69th   2017

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  • Rab7によるオートファジー制御機構の再評価

    朽津芳彦, 藤田尚信, 福田光則

    日本細胞生物学会大会(Web)   69th   2017

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  • アミノ酸飢餓により誘導されるオートリソソームの成熟機構

    朽津芳彦, 藤田尚信, 福田光則

    日本生化学会大会(Web)   90th   2017

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  • Theオートファジー 研究者たちの集大成が見える最新ビジュアルテキスト 第2章 オートファジーの分子機構 3.Rabによるオートファジー制御

    朽津芳彦, 藤田尚信, 福田光則

    実験医学   35 ( 15 )   2017

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  • 【炎症と免疫におけるオートファジーの新たな側面】バクテリアの侵入時にみられるユビキチン化とAtg蛋白質の局在化機構

    藤田 尚信, 吉森 保

    炎症と免疫   20 ( 2 )   146 - 150   2012.2

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    Language：Japanese   Publisher：(株)先端医学社  

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  • Atg12-5/16L1複合体によるRab33B依存的膜輸送制御の可能性について

    伊藤敬, 藤田尚信, 齊藤達哉, 小松雅明, 審良静男, 吉森保, 福田光則

    日本分子生物学会年会プログラム・要旨集(Web)   35th   2012

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  • オートファジー 分子機構と疾患との関わり

    藤田 尚信, 吉森 保

    BIO Clinica   26 ( 4 )   369 - 372   2011.4

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  • 【疾患に対抗するオートファジー 感染防御、免疫制御の新規メカニズムから糖尿病、パーキンソン病への関与まで】オートファジーの駆動・制御機構の進化と疾患とのかかわり

    松永 耕一, 藤田 尚信, 吉森 保

    実験医学   27 ( 18 )   2930 - 2936   2009.11

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    Language：Japanese   Publisher：(株)羊土社  

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  • Regulation of innate immune response by an autophagy-related protein

    Tatsuya Saitoh, Naonobu Fujita, Tamotsu Yoshimori, Shizuo Akira

    AUTOPHAGY   5 ( 6 )   909 - 909   2009.8

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    Language：English   Publishing type：Research paper, summary (international conference)  

    Web of Science

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  • 【オートファジー メカニズムと生理機能】オートファジーと炎症

    齊藤 達哉, 藤田 尚信, 吉森 保, 審良 静男

    細胞   41 ( 7 )   283 - 286   2009.7

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    Language：Japanese   Publisher：(株)ニュー・サイエンス社  

    J-GLOBAL

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  • 【感染現象 その理解の深化から疾患制御への展望】生体防御機構研究の新展開 オートファジーによる炎症反応制御

    齊藤 達哉, 藤田 尚信, 吉森 保, 審良 静男

    蛋白質・核酸・酵素   54 ( 8 )   1119 - 1124   2009.6

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    Language：Japanese   Publisher：共立出版(株)  

    CiNii Books

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  • オートファジー関連因子による自然免疫応答の制御

    齊藤達哉, 齊藤達哉, 藤田尚信, 吉森保, 審良静男, 審良静男

    日本分子生物学会年会講演要旨集   32nd ( Vol.2 )   2009

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  • 【メンブレントラフィックの奔流 分子から細胞、そして個体へ】メンブレントラフィックと高次機能 メンブレントラフィックと感染・免疫 オートファジーと自然免疫応答

    齊藤 達哉, 藤田 尚信, 吉森 保, 審良 静男

    蛋白質・核酸・酵素   53 ( 16 )   2279 - 2285   2008.12

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    CiNii Books

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    Other Link： http://search.jamas.or.jp/link/ui/2009056223

  • 【メンブレントラフィックの奔流 分子から細胞、そして個体へ】メンブレントラフィックの分子メカニズム 哺乳類オートファジー研究の夜明け

    藤田 尚信, 松永 耕一, 野田 健司, 吉森 保

    蛋白質・核酸・酵素   53 ( 16 )   2106 - 2110   2008.12

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  • タンパク質分解を介した新たな生理機能 オートファジー関連分子Atg16L1はエンドトキシンによるインフラマソーム活性化を制御する(Atg16L1, an autophagy protein, controls endotoxin-induced inflammasome activation)

    齊藤 達哉, 藤田 尚信, 張 明浩, 植松 智, 梁 甫伎, 佐藤 荘, 大森 弘子, 野田 健司, 山本 直樹, 小松 雅明, 田中 啓二, 河合 太郎, 辻村 亨, 竹内 理, 吉森 保, 審良 静男

    日本生化学会大会・日本分子生物学会年会合同大会講演要旨集   81回・31回   4S3 - 7   2008.11

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    Language：English   Publisher：(公社)日本生化学会  

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  • 哺乳類オートファジー研究の夜明け

    藤田尚信, 松永耕一, 野田健司, 吉森保

    蛋白質核酸酵素 増刊 メンブレントラフィックの奔流、１２月号増刊   2008

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Research Projects

  • ポストリソソーム生物学研究領域の創成支援

    Grant number：21H05144  2021.8 - 2024.3

    日本学術振興会  科学研究費助成事業  学術変革領域研究(B)

    中村 修平, 藤田 尚信, 吉川 治孝, 永沼 達郎

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    Grant amount：\4420000 （ Direct Cost: \3400000 、 Indirect Cost：\1020000 ）

    ポストリソソーム生物学研究を推進するため、slackを使った関連情報の共有や３ヶ月に一回のwebベースのミーテイングでの進捗報告を通してメンバー間で緊密な連携をとる体制を構築した。また、アドバイザーの先生を交えたキックオフミーティングを開催し、研究の方向性に関する助言を得た。領域の概要や活動報告についてHPを作製(https://post-lysosome.jp/)して情報発信を開始した。

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  • 体液のマルチオミクス解析による寿命を制御するポストリソソーム経路の解明

    Grant number：21H05147  2021.8 - 2024.3

    日本学術振興会  科学研究費助成事業  学術変革領域研究(B)

    藤田 尚信, 吉川 治孝

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    Grant amount：\33150000 （ Direct Cost: \25500000 、 Indirect Cost：\7650000 ）

    細胞内の分解の場であるリソソームが生存・寿命を制御するシグナルを発信するという新しいコンセプトが生まれつつある。しかしながら、どの臓器からどのようなポストリソソームシグナルが発信されているのか、その実体は明らかにされていない。本研究では、ポストリソソームシグナルの起点となる臓器を同定すると共に、開放血管系を持つショウジョウバエの利点を生かした体液の比較マルチオミクス解析により、寿命延長につながる体液中のポストリソソームメディエーターの網羅的な同定を目指している。
    体液中のポストリソソームメディエーターを同定するため、野生型、オートファジー不全系統、またリソソーム機能が低下した変異体より体液を回収し、体液の比較プロテオミクスを実施し、オートファジー・リソソーム機能の低下により存在量が有意に変動する一群のタンパク質を同定した。また、寿命延長につながるポストリソソームシグナルの起点となる臓器を探索するためのツールを整備した。

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  • 管状リソソームネットワークの形成メカニズムと機能の解明

    Grant number：21H02473  2021.4 - 2024.3

    日本学術振興会  科学研究費助成事業  基盤研究(B)

    藤田 尚信

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    Grant amount：\12480000 （ Direct Cost: \9600000 、 Indirect Cost：\2880000 ）

    リソソームは球状のオルガネラであるが、特定の条件下では形態を変化させることが知られている。しかしながら、そのメカニズムや機能はこれまで十分に明らかにされていない。私たちは、ショウジョウバエの変態期に腹部の筋細胞に管状のリソソームネットワークが形成されることを見出した。本研究では、ショウジョウバエの遺伝学やトランスクリプトーム解析などを駆使し、筋細胞に見られる管状リソソームネットワークの形成メカニズムとその生物学的意義の解明を目指している。
    リソソームの管状化に働く遺伝子を選別するため、管状リソソームネットワークが形成される腹部筋細胞の経時的なトランスクリプトーム解析を実施し、筋細胞リモデリングに伴う遺伝子の発現変動を明らかにした。それらの中から、管状リソソームネットワークが形成されるタイミングに発現の高いものを選別し、in vivo RNAiスクリーニングに供した。その結果、ノックダウンすることにより、管状リソソームの形成を抑える複数の遺伝子を新たに同定することに成功した。

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  • リソソーム膜タンパク質のリソソーム内分解メカニズムの解析

    Grant number：20H05315  2020.4 - 2022.3

    日本学術振興会  科学研究費助成事業  新学術領域研究(研究領域提案型)

    藤田 尚信

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    Grant amount：\8970000 （ Direct Cost: \6900000 、 Indirect Cost：\2070000 ）

    分解の場であるリソソームの活性調節には、酸性加水分解酵素のみでなくリソソームに局在する膜タンパク質の品質管理も重要である。しかしながら、リソソーム膜タンパク質がどのように分解・代謝されているのか、その実体は驚くほど明らかにされていない。本研究では、ショウジョウバエ個体を用いた独自の解析系を利用し、リソソーム膜タンパク質がリソソーム内腔に取り込まれ分解される実体の解明を目指した。
    RFPが酸性条件下でも消光しないという特性を利用することにより、ヒトの肝臓と脂肪の機能を併せ持つショウジョウバエ幼虫の脂肪体において、リソソーム膜タンパク質であるLampがリソソーム内で分解されていることを見出した。また、その分解は幼虫最後期の脂肪体ではほとんど見られないことが判明した。そのメカニズムの解析から、幼虫最後期に体内濃度が上昇する変態ホルモンであるエクダイソンにより、リソソーム活性およびリソソーム膜タンパク質の内腔への取り込みが抑えられていることが明らかになった。

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  • Functional analysis of the tubular lysosomal network in muscle cell

    Grant number：18K06202  2018.4 - 2021.3

    Japan Society for the Promotion of Science  Grants-in-Aid for Scientific Research  Grant-in-Aid for Scientific Research (C)

    Fujita Naonobu

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    Grant amount：\4420000 （ Direct Cost: \3400000 、 Indirect Cost：\1020000 ）

    The shape of lysosomes changeswith cellular degradative demands; however, there is limited knowledge about the mechanisms or significance that underlies distinct lysosomal morphologies. Here, we found an extensive tubular autolysosomal network in Drosophila abdominal muscle remodeling during metamorphosis. The tubular network transiently appeared and exhibited the capacity to degrade autophagic cargoes. The tubular autolysosomal network formation depended on both autophagic flux and degradative function, with the exception of the Atg12 and Atg8 ubiquitin-like conjugation systems. Among ATG deficient mutants, the efficiency of lysosomal tubulation correlated with the phenotypic severity in muscle remodeling. The lumen of the tubular network was continuous and homogeneous across a broad region of the remodeling muscle. Altogether, we revealed that the dynamic expansion of a tubular autolysosomal network synchronizes the abundant degradative activity.

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  • オートファジーによる不良タンパク質の選択的分解機構―アダプター仮説の検証

    Grant number：22020023  2010 - 2011

    日本学術振興会  科学研究費助成事業  特定領域研究

    藤田 尚信, 森田 英嗣

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    Grant amount：\6400000 （ Direct Cost: \6400000 ）

    これまで易凝集性タンパク質や病原性微生物などのオートファジーの選択的基質p62などのアダプタータンパク質を介してオートファゴソーム局在タンパク質LC3と結合し、選択的に分解されると考えられている。しかしながらその分子機構には十分に検証されていない。そこで我々は、オートファジー関連因子(ATG遺伝子)をノックアウトした一連の細胞を用いて、Atgタンパク質の基質への局在階層性を解析した。その結果、これまでのモデルとは大きく異なり、LC3に依存せずに他のAtgタンパク質が選択的基質上に局在することを明らかにした。その中でも選択性に重要であると考えられるAtg16L1複合体の局在化機構に焦点を絞りさらに解析を進めた。Atg16L1複合体はLC3システムのE3様因子として働く因子である(Fujita et al.,2008)。基質選択的オートファジーにはユビキチン化が重要であると考えられていることから、Atg16L1とユビキチンとの結合の有無を調べたところ、Atg16L1分子はC末端側の機能未知のWDリピートドメインを介してユビキチン鎖と直接結合した。さらに我々は、Atg16L1はFIP200(酵母Atg17の哺乳類ホモログ)とも直接結合することを見出した。ユビキチン、FIP200それぞれ片方との結合を抑えても大きな影響は見られないが、双方との結合能を失わせたAtg16L1を発現させた細胞ではオートファジー能は有意に低下した。これらの結果から、Atg16L1複合体はユビキチンとFIP200との結合を介して選択的基質上に局在していると考えられる。このように今回の結果から、LC3やアダプタータンパク質に依存しない選択的オートファジーの新たな分子機構が明らかになった。

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  • Ubiquitination mediated autophagy against invading bacteria

    Grant number：22770194  2010 - 2011

    Japan Society for the Promotion of Science  Grants-in-Aid for Scientific Research  Grant-in-Aid for Young Scientists (B)

    FUJITA Naonobu

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    Grant amount：\4290000 （ Direct Cost: \3300000 、 Indirect Cost：\990000 ）

    Although ubiquitination is thought to be important for the autophagic response to invading bacteria(also called xenophagy), it remains enigmatic whether ubiquitin is conjugated to bacterial proteins or host cellular proteins. Here we found that rupture of endosome by bacterial toxin or transfection reagent leads to ubiquitination of host cellular endosomal proteins, and that is sufficient for induction of selective autophagy.

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  • Functional analysis of the WD repeats domain in Atg16L which associates with Crohn disease

    Grant number：20870027  2008 - 2009

    Japan Society for the Promotion of Science  Grants-in-Aid for Scientific Research  Grant-in-Aid for Young Scientists (Start-up)

    FUJITA Naonobu

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    Grant amount：\3302000 （ Direct Cost: \2540000 、 Indirect Cost：\762000 ）

    Recent genome-wide association studies have linked autophagy, an intracellular bulk degradation system essential for diverse physiological process, with Crohn's disease, a major form of chronic inflammatory bowel disease. Single nucleotide polymorphisms in Atg16L (T300A) is a risk factor for Crohn's disease. However, it has been ill defined how the Atg16L variant confers the development of the disease. We demonstrate that Atg16L is a critical regulator of autophagy responsible for the control of the endotoxin-mediated immune response ; its dysfunction may be associated with inflammatory diseases such as colitis. Furthermore, we provide the first evidence that deletion of WD repeat domain and T300A mutation in Atg16L1 have little impact on canonical autophagy and autophagy against bacteria, Salmonella typhimurium. We therefore propose that Atg16L1 T300A is differentially involved in Crohn's disease and canonical autophagy.

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