研究者データベース

茂木 文夫(モテギ フミオ)
遺伝子病制御研究所 病態研究部門
教授

基本情報

所属

  • 遺伝子病制御研究所 病態研究部門

職名

  • 教授

科研費研究者番号

  • 10360653

J-Global ID

研究キーワード

  • 胚発生   メカノバイオロジー   細胞極性   

研究分野

  • ライフサイエンス / 生物物理学 / メカノバイオロジー
  • ライフサイエンス / 発生生物学 / 胚発生
  • ライフサイエンス / 細胞生物学 / 細胞極性

職歴

  • 2020年10月 - 現在 北海道大学 遺伝子病制御研究所 発生生理学分野 教授
  • 2012年08月 - 2021年03月 シンガポール国立大学 理学部 生物学科 准教授
  • 2012年08月 - 2021年03月 シンガポール国立大学 メカノバイオロジー研究所 主任研究員
  • 2012年08月 - 2021年03月 テマセク生命科学研究所 主幹主任研究員
  • 2007年08月 - 2012年07月 ジョンズホプキンス大学 医学部 研究員
  • 2006年08月 - 2007年07月 カリフォルニア大学サンディエゴ校 研究員
  • 2002年04月 - 2006年07月 理化学研究所 発生再生科学研究センター 研究員

学歴

  • 1997年04月 - 2002年03月   東京大学   大学院総合文化研究科   生命環境科学系

研究活動情報

論文

  • Wan Jun Gan, Fumio Motegi
    Frontiers in Cell and Developmental Biology 8 2021年01月18日 
    Cell polarity is the asymmetric organization of cellular components along defined axes. A key requirement for polarization is the ability of the cell to break symmetry and achieve a spatially biased organization. Despite different triggering cues in various systems, symmetry breaking (SB) usually relies on mechanochemical modulation of the actin cytoskeleton, which allows for advected movement and reorganization of cellular components. Here, the mechanisms underlying SB in Caenorhabditis elegans zygote, one of the most popular models to study cell polarity, are reviewed. A zygote initiates SB through the centrosome, which modulates mechanics of the cell cortex to establish advective flow of cortical proteins including the actin cytoskeleton and partitioning defective (PAR) proteins. The chemical signaling underlying centrosomal control of the Aurora A kinase–mediated cascade to convert the organization of the contractile actomyosin network from an apolar to polar state is also discussed.
  • Fumio Motegi, Nicolas Plachta, Virgile Viasnoff
    Current Opinion in Cell Biology 62 78 - 85 2020年02月
  • Peng Zhao, Xiang Teng, Sarala Neomi Tantirimudalige, Masatoshi Nishikawa, Thorsten Wohland, Yusuke Toyama, Fumio Motegi
    Developmental Cell 48 5 631 - 645.e6 2019年03月
  • Ravikrishna Ramanujam, Ziyin Han, Zhen Zhang, Pakorn Kanchanawong, Fumio Motegi
    Nature Chemical Biology 14 10 917 - 927 2018年10月
  • Sriyash Mangal, Jennifer Sacher, Taekyung Kim, Daniel Sampaio Osório, Fumio Motegi, Ana Xavier Carvalho, Karen Oegema, Esther Zanin
    Journal of Cell Biology 217 3 837 - 848 2018年03月05日 
    During cytokinesis, a signal from the central spindle that forms between the separating anaphase chromosomes promotes the accumulation of contractile ring components at the cell equator, while a signal from the centrosomal microtubule asters inhibits accumulation of contractile ring components at the cell poles. However, the molecular identity of the inhibitory signal has remained unknown. To identify molecular components of the aster-based inhibitory signal, we developed a means to monitor the removal of contractile ring proteins from the polar cortex after anaphase onset. Using this assay, we show that polar clearing is an active process that requires activation of Aurora A kinase by TPXL-1. TPXL-1 concentrates on astral microtubules coincident with polar clearing in anaphase, and its ability to recruit Aurora A and activate its kinase activity are essential for clearing. In summary, our data identify Aurora A kinase as an aster-based inhibitory signal that restricts contractile ring components to the cell equator during cytokinesis.
  • Zhen Zhang, Yen Wei Lim, Peng Zhao, Pakorn Kanchanawong, Fumio Motegi
    Journal of Cell Science 130 24 4200 - 4212 2017年12月15日
  • Ravikrishna Ramanujam, Tricia Yu Feng Low, Yen Wei Lim, Fumio Motegi
    Seminars in Cell & Developmental Biology 71 129 - 136 2017年11月
  • Shyi-Chyi Wang, Tricia Yu Feng Low, Yukako Nishimura, Laurent Gole, Weimiao Yu, Fumio Motegi
    Nature Cell Biology 19 8 988 - 995 2017年08月
  • Yukinobu Arata, Michio Hiroshima, Chan-Gi Pack, Ravikrishna Ramanujam, Fumio Motegi, Kenichi Nakazato, Yuki Shindo, Paul W. Wiseman, Hitoshi Sawa, Tetsuya J. Kobayashi, Hugo B. Brandão, Tatsuo Shibata, Yasushi Sako
    Cell Reports 17 1 316 - 316 2016年09月
  • Fumio Motegi, Geraldine Seydoux
    Philosophical Transactions of the Royal Society B: Biological Sciences 368 1629 20130010 - 20130010 2013年11月05日 
    To become polarized, cells must first ‘break symmetry’. Symmetry breaking is the process by which an unpolarized, symmetric cell develops a singularity, often at the cell periphery, that is used to develop a polarity axis. The Caenorhabditis elegans zygote breaks symmetry under the influence of the sperm-donated centrosome, which causes the PAR polarity regulators to sort into distinct anterior and posterior cortical domains. Modelling analyses have shown that cortical flows induced by the centrosome combined with antagonism between anterior and posterior PARs (mutual exclusion) are sufficient, in principle, to break symmetry, provided that anterior and posterior PAR activities are precisely balanced. Experimental evidence indicates, however, that the system is surprisingly robust to changes in cortical flows, mutual exclusion and PAR balance. We suggest that this robustness derives from redundant symmetry-breaking inputs that engage two positive feedback loops mediated by the anterior and posterior PAR proteins. In particular, the PAR-2 feedback loop stabilizes the polarized state by creating a domain where posterior PARs are immune to exclusion by anterior PARs. The two feedback loops in the PAR network share characteristics with the two feedback loops in the Cdc42 polarization network of Saccharomyces cerevisiae .
  • Microtubules induce self-organization of polarized PAR domains in Caenorhabditis elegans zygotes
    Fumio Motegi, Seth Zonies, Yingsong Hao, Adrian A Cuenca, Erik Griffin, Geraldine Seydoux
    Nature Cell Biology 13 11 1361 - 1367 2011年10月 [査読有り]
  • Shinji Ihara, Elliott J. Hagedorn, Meghan A. Morrissey, Qiuyi Chi, Fumio Motegi, James M. Kramer, David R. Sherwood
    Nature Cell Biology 13 6 641 - 651 2011年06月
  • C. M. Gallo, J. T. Wang, F. Motegi, G. Seydoux
    Science 330 6011 1685 - 1689 2010年12月17日
  • Caenorhabditis elegans ortholog of the p24/p22 subunit, DNC-3, is essential for the formation of the dynactin complex by bridging DNC-1/p150(Glued) and DNC-2/dynamitin
    Masahiro Terasawa, Mika Toya, Fumio Motegi, Miyeko Mana, Kuniaki Nakamura, Asako Sugimoto
    Genes to Cells 15 11 1145 - 1157 2010年11月
  • S. Zonies, F. Motegi, Y. Hao, G. Seydoux
    Development 137 10 1669 - 1677 2010年05月15日
  • R. Gassmann, A. Essex, J.-S. Hu, P. S. Maddox, F. Motegi, A. Sugimoto, S. M. O'Rourke, B. Bowerman, I. McLeod, J. R. Yates, K. Oegema, I. M. Cheeseman, A. Desai
    Genes & Development 22 17 2385 - 2399 2008年09月01日
  • Revisiting the role of microtubules in C. elegans polarity.
    Motegi F, Seydoux G
    Journal of Cell Biology 179 3 367 - 369 2007年11月
  • Function of microtubules at the onset of cytokinesis
    Fumio Motegi, Asako Sugimoto
    Tanpakusitu Kakusan Koso 51 1590 - 1595 2006年09月
  • Cell polarization: lessons from C. elegans asymmetric cell division
    Fumio Motegi, Asako Sugimoto
    Tanpakushitsu Kakusan Koso 51 776 - 781 2006年05月
  • Two phases of astral microtubule activity during cytokinesis in C. elegans embryos
    Motegi F, Velarde NV, Piano F, Sugimoto A
    Developmental Cell 10 4 509 - 520 2006年04月
  • Fumio Motegi, Mithilesh Mishra, Mohan K. Balasubramanian, Issei Mabuchi
    Journal of Cell Biology 165 5 685 - 695 2004年06月07日 
    Cytokinesis in many eukaryotes requires an actomyosin contractile ring. Here, we show that in fission yeast the myosin-II heavy chain Myo2 initially accumulates at the division site via its COOH-terminal 134 amino acids independently of F-actin. The COOH-terminal region can access to the division site at early G2, whereas intact Myo2 does so at early mitosis. Ser1444 in the Myo2 COOH-terminal region is a phosphorylation site that is dephosphorylated during early mitosis. Myo2 S1444A prematurely accumulates at the future division site and promotes formation of an F-actin ring even during interphase. The accumulation of Myo2 requires the anillin homologue Mid1 that functions in proper ring placement. Myo2 interacts with Mid1 in cell lysates, and this interaction is inhibited by an S1444D mutation in Myo2. Our results suggest that dephosphorylation of Myo2 liberates the COOH-terminal region from an intramolecular inhibition. Subsequently, dephosphorylated Myo2 is anchored by Mid1 at the medial cortex and promotes the ring assembly in cooperation with F-actin.
  • Kelvin C.Y. Wong, Ventris M. D'souza, Naweed I. Naqvi, Fumio Motegi, Issei Mabuchi, Mohan K. Balasubramanian
    Current Biology 12 9 724 - 729 2002年04月
  • Contractile ring formation in Xenopus egg and fission yeast
    Noguchi T, Arai R, Motegi F, Nakano K, Mabuchi I
    Cell Structure and Function 26 6 545 - 554 2001年12月
  • Identification of two type V myosins in fission yeast, one of which functions in polarized cell growth and moves rapidly in the cell.
    Motegi F, Arai R, Mabuchi I
    Molecular Biology of the Cell 12 5 1367 - 1380 2001年05月
  • Identification and functional analysis of the gene for type I myosin in fission yeast
    Toya M, Motegi F, Nakano K, Mabuchi I, Yamamoto M
    Genes to Cells 62 3 187 - 199 2001年03月
  • The S. pombe rlc1 gene encodes a putative myosin regulatory light chain that binds the type II myosins myo3p and myo2p
    Le Goff, Motegi F, Salimova E, Mabuchi I, Simanis V
    113 4157 - 4163 2000年12月
  • Molecular mechanism of myosin-II assembly at the division site in Schizosaccharomyces pombe
    F Motegi, K Nakano, I Mabuchi
    Journal of Cell Science 113 1813 - 1825 2000年05月
  • Masako Suda, Mikiko Fukui, Yuki Sogabe, Kazuhito Sato, Akeshi Morimatsu, Ritsuko Arai, Fumio Motegi, Tokichi Miyakawa, Issei Mabuchi, Dai Hirata
    Genes to Cells 4 9 517 - 527 1999年09月
  • Fumio Motegi, Kentaro Nakano, Chikako Kitayama, Masayuki Yamamoto, Issei Mabuchi
    FEBS Letters 420 2-3 161 - 166 1997年12月29日

書籍

  • ラボレポート独立編: 在新加坡的自立門户之路: シンガポールで独立してみた
    茂木文夫 
    実験医学 2019年06月

受賞

  • 2010年05月 日本細胞生物学会 若手最優秀発表賞


Copyright © MEDIA FUSION Co.,Ltd. All rights reserved.