Curved EFC/F-BAR-domain dimers are joined end to end into a filament for membrane invagination in endocytosis

Cell. 2007 May 18;129(4):761-72. doi: 10.1016/j.cell.2007.03.040.

Atsushi Shimada ¹, Hideaki Niwa, Kazuya Tsujita, Shiro Suetsugu, Koji Nitta, Kyoko Hanawa-Suetsugu, Ryogo Akasaka, Yuri Nishino, Mitsutoshi Toyama, Lirong Chen, Zhi-Jie Liu, Bi-Cheng Wang, Masaki Yamamoto, Takaho Terada, Atsuo Miyazawa, Akiko Tanaka, Sumio Sugano, Mikako Shirouzu, Kuniaki Nagayama, Tadaomi Takenawa, Shigeyuki Yokoyama

Affiliations

Affiliation

1 RIKEN SPring-8 Center, Harima Institute, 1-1-1 Kouto, Sayo, Hyogo 679-5148, Japan.

PMID: 17512409 DOI: 10.1016/j.cell.2007.03.040

Abstract

Pombe Cdc15 homology (PCH) proteins play an important role in a variety of actin-based processes, including clathrin-mediated endocytosis (CME). The defining feature of the PCH proteins is an evolutionarily conserved EFC/F-BAR domain for membrane association and tubulation. In the present study, we solved the crystal structures of the EFC domains of human FBP17 and CIP4. The structures revealed a gently curved helical-bundle dimer of approximately 220 A in length, which forms filaments through end-to-end interactions in the crystals. The curved EFC dimer fits a tubular membrane with an approximately 600 A diameter. We subsequently proposed a model in which the curved EFC filament drives tubulation. In fact, striation of tubular membranes was observed by phase-contrast cryo-transmission electron microscopy, and mutations that impaired filament formation also impaired membrane tubulation and cell membrane invagination. Furthermore, FBP17 is recruited to clathrin-coated pits in the late stage of CME, indicating its physiological role.

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