A Novel Membrane Fission Mechanism by Dynamin Complex: Clusterase Model

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  • TAKEI Kohji
    Division of Biochemistry, Department of Neuroscience, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences
  • YAMADA Hiroshi
    Division of Biochemistry, Department of Neuroscience, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences
  • TAKEDA Tetsuya
    Division of Biochemistry, Department of Neuroscience, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences

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Other Title
  • ダイナミン複合体による新規の膜切断機構：クラスタラーゼ・モデル
  • ダイナミン フクゴウタイ ニ ヨル シンキ ノ マク セツダン キコウ : クラスタラーゼ ・ モデル

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Abstract

<p>Dynamin GTPase, an essential endocytotic protein, helically polymerizes at the neck of endocytic pits, and mechanically sever the membrane upon GTP hydrolysis. However, it is not known exactly how the dynamin disconnect the membrane. To clarify the mechanisms we analyzed structural changes of dynamin complexes during membrane fission using electron microscopy and high-speed atomic force microscopy (HS-AFM). Surprisingly, the dynamin ring complexes were clustered upon GTP hydrolysis and membrane constriction occurred at uncoated regions between the clusters, suggesting a novel mode of action of dynamin. In this commentary, we illustrate dynamin’s membrane fission models proposed thus far, and our novel “clusterase” model.</p>

Journal

  • Seibutsu Butsuri

    Seibutsu Butsuri 59 (5), 255-261, 2019

    The Biophysical Society of Japan General Incorporated Association

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