Structure-Function Analysis of the EFC/F-BAR Domain-Mechanism of Membrane Invagination in Endocytosis-

DOI Web Site 16 References
  • SHIMADA Atsushi
    Division of Synchrotron Radiation Instrumentation, RIKEN SPring-8 Center, Harima Institute
  • SUETSUGU Shiro
    Laboratory of Membrane and Cytoskeleton Dynamics Frontier Research Program for Young Investigators, Institute of Molecular and Cellular Biosciences, the University of Tokyo
  • SHIROUZU Mikako
    Systems and Structural Biology Center, Yokohama Institute, RIKEN
  • NAGAYAMA Kuniaki
    Okazaki Institute for Integrative Bioscience, National Institutes of Natural Sciences
  • YOKOYAMA Shigeyuki
    Systems and Structural Biology Center, Yokohama Institute, RINEN

Bibliographic Information

Other Title
  • ＥＦＣ／Ｆ‐ＢＡＲドメインの構造機能解析―エンドサイトーシスにおける細胞膜陥入機構―
  • EFC F BAR ドメイン ノ コウゾウ キノウ カイセキ エンドサイトーシス ニ オケル サイボウマク カンニュウ キコウ
  • —Mechanism of Membrane Invagination in Endocytosis—
  • ―エンドサイト―シスにおける細胞膜陥入機構―

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Abstract

Pombe Cdc 15 homology (PCH) proteins are involved in a variety of actin-based processes, including clathrin-mediated endocytosis. The PCH proteins contain an evolutionarily conserved, EFC/F-BAR domain for membrane association and tubulation. We solved the crystal structures of the EFC domains of human FBP 17 and CIP4. The structures revealed a gently-curved helicalbundle dimer, which forms filaments through end-to-end interactions in the crystals. The structural and biochemical data suggested a mechanistic model, in which the curved EFC filament drives tubulation. The electron micrographs of the EFC-induced tubular membranes supported this model. The physiological role of the EFC domain in clathrin-mediated endocytosis is discussed.

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