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
N1 - Funding Information:
We thank S. Morita, Y. Kinoshita, K. Nagano, H. Tochio-Uda, N. Maoka, Y. Tomabechi, H. Hamana, N. Obayashi, S. Tojo, M. Ueno, S. Oojimi, K. Honda, K. Usui, M. Aoki, M. Inoue, K. Katsura, and T. Tanaka for sample preparations and Drs. R. Danev and H. Shigematsu for help in the cryo-TEM data collection and for fruitful discussions. We thank Dr. T. Itoh (Institute of Medical Science, The University of Tokyo) for technical support and helpful discussions. We also thank Dr. K. Toyooka and his colleagues at the RIKEN Plant Science Center for electron microscopy. X-ray data were collected at the RIKEN Structural Genomics Beamline I (BL26B1) at SPring-8 and at the Southeast Regional Collaborative Access Team (SER-CAT) 22-ID beamline at the Advanced Photon Source, Argonne National Laboratory. Supporting institutions may be found at http://www.ser.anl.gov/new/members.html . Use of the Advanced Photon Source was supported by the US Department of Energy, Office of Science, Office of Basic Energy Sciences under Contract No. W-31-109-Eng-38. This work was supported by the RIKEN Structural Genomics/Proteomics Initiative (RSGI), the National Project on Protein Structural and Functional Analyses, Ministry of Education, Culture, Sports, Science and Technology of Japan. This work was also supported by grants-in-aid for Scientific Research on Priority Areas from the Ministry of Education, Culture, Sports, and Technology of Japan and from the Japan Science and Technology Corporation (JST).
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 -