TY - JOUR
T1 - Curved EFC/F-BAR-Domain Dimers Are Joined End to End into a Filament for Membrane Invagination in Endocytosis
AU - Shimada, Atsushi
AU - Niwa, Hideaki
AU - Tsujita, Kazuya
AU - Suetsugu, Shiro
AU - Nitta, Koji
AU - Hanawa-Suetsugu, Kyoko
AU - Akasaka, Ryogo
AU - Nishino, Yuri
AU - Toyama, Mitsutoshi
AU - Chen, Lirong
AU - Liu, Zhi Jie
AU - Wang, Bi Cheng
AU - Yamamoto, Masaki
AU - Terada, Takaho
AU - Miyazawa, Atsuo
AU - Tanaka, Akiko
AU - Sugano, Sumio
AU - Shirouzu, Mikako
AU - Nagayama, Kuniaki
AU - Takenawa, Tadaomi
AU - Yokoyama, Shigeyuki
PY - 2007/5/18
Y1 - 2007/5/18
N2 - 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.
AB - 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.
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U2 - 10.1016/j.cell.2007.03.040
DO - 10.1016/j.cell.2007.03.040
M3 - Article
C2 - 17512409
AN - SCOPUS:34249316521
VL - 129
SP - 761
EP - 772
JO - Cell
JF - Cell
SN - 0092-8674
IS - 4
ER -