Article
- The EMBO Journal (2006) 25, 2889 - 2897
- doi:10.1038/sj.emboj.7601176
Published online: 8 June 2006
Subject Categories:
Endophilin BAR domain drives membrane curvature by two newly identified structure-based mechanisms
Michitaka Masuda1,a, Soichi Takeda2,3,a, Manami Sone1, Takashi Ohki1, Hidezo Mori2, Yuji Kamioka1 and Naoki Mochizuki1
- Department of Structural Analysis, National Cardiovascular Center Research Institute, Suita, Osaka, Japan
- Department of Cardiac Physiology, National Cardiovascular Center Research Institute, Suita, Osaka, Japan
- Laboratory of structural biochemistry, RIKEN Harima Institute at SPring-8, Mikazuki-cho, Sayo, Hyogo, Japan
Correspondence to:
Naoki Mochizuki, Department of Structural Analysis, National Cardiovascular Center Research Institute, 5-7-1 Fujishiro-dai, Suita, Osaka 565-8565, Japan. Tel.: +81 6 6833 5012; Fax: +81 6 6835 5461; E-mail: nmochizu@ri.ncvc.go.jp
aThese authors contributed equally to this work
Received 15 November 2005; Accepted 8 May 2006
Abstract
The crescent-shaped BAR (Bin/Amphiphysin/Rvs-homology) domain dimer is a versatile protein module that senses and generates positive membrane curvature. The BAR domain dimer of human endophilin-A1, solved at 3.1 Å, has a unique structure consisting of a pair of helix–loop appendages sprouting out from the crescent. The appendage's short helices form a hydrophobic ridge, which runs across the concave surface at its center. Examining liposome binding and tubulation in vitro using purified BAR domain and its mutants indicated that the ridge penetrates into the membrane bilayer and enhances liposome tubulation. BAR domain-expressing cells exhibited marked plasma membrane tubulation in vivo. Furthermore, a swinging-arm mutant lost liposome tubulation activity yet retaining liposome binding. These data suggested that the rigid crescent dimer shape is crucial for the tubulation. We here propose that the BAR domain drives membrane curvature by coordinate action of the crescent's scaffold mechanism and the ridge's membrane insertion in addition to membrane binding via amino-terminal amphipathic helix.
Keywords:
- BAR domain,
- endophilin,
- liposome,
- membrane curvature,
- membrane insertion
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