| Literature DB >> 17512409 |
Atsushi Shimada1, 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.
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.Entities:
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Year: 2007 PMID： 17512409 DOI： 10.1016/j.cell.2007.03.040
Source DB: PubMed Journal: Cell ISSN： 0092-8674 Impact factor: 41.582