Curved EFC/F-BAR-Domain Dimers Are Joined End to End into a Filament for Membrane Invagination in Endocytosis

Atsushi Shimada, 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 TakenawaShigeyuki Yokoyama

Research output: Contribution to journalArticlepeer-review

345 Citations (Scopus)


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 ∼220 Å in length, which forms filaments through end-to-end interactions in the crystals. The curved EFC dimer fits a tubular membrane with an ∼600 Å 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.

Original languageEnglish
Pages (from-to)761-772
Number of pages12
Issue number4
Publication statusPublished - May 18 2007
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • General Biochemistry,Genetics and Molecular Biology


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