Article
- The EMBO Journal (2008) 27, 2817 - 2828
- doi:10.1038/emboj.2008.216
Published online: 16 October 2008
Subject Categories:
EFC/F-BAR proteins and the N-WASP–WIP complex induce membrane curvature-dependent actin polymerization
Kazunari Takano1, Kiminori Toyooka2 and Shiro Suetsugu1,3
- Laboratory of Membrane and Cytoskeleton Dynamics, Institute of Molecular and Cellular Biosciences, The University of Tokyo, Tokyo, Japan
- Gene Discovery Research Group, RIKEN Plant Science Center, Yokohama, Japan
- PRESTO, Japan Science and Technology Agency, Kawaguchi-shi, Japan
Correspondence to:
Shiro Suetsugu, Laboratory of Membrane and Cytoskeleton Dynamics, Institute of Molecular and Cellular Biosciences, The University of Tokyo, 1-1-1, Yayoi, Bunkyo-ku, Tokyo 113-0032, Japan. Tel.: +81 3 5841 7954; Fax: +81 3 5841 7862; E-mail: suetsugu@iam.u-tokyo.ac.jp
Received 22 July 2008; Accepted 22 September 2008
Abstract
Extended Fer-CIP4 homology (EFC)/FCH-BAR (F-BAR) domains generate and bind to tubular membrane structures of defined diameters that are involved in the formation and fission of endocytotic vesicles. Formin-binding protein 17 (FBP17) and Toca-1 contain EFC/F-BAR domains and bind to neural Wiskott–Aldrich syndrome protein (N-WASP), which links phosphatidylinositol (4,5)-bisphosphate (PIP2) and the Rho family GTPase Cdc42 to the Arp2/3 complex. The N-WASP–WASP-interacting protein (WIP) complex, a predominant form of N-WASP in cells, is known to be activated by Toca-1 and Cdc42. Here, we show that N-WASP–WIP complex-mediated actin polymerization is activated by phosphatidylserine-containing membranes depending on membrane curvature in the presence of Toca-1 or FBP17 and in the absence of Cdc42 and PIP2. Cdc42 further promoted the activation of actin polymerization by N-WASP–WIP. Toca-1 or FBP17 recruited N-WASP–WIP to the membrane. Conserved acidic residues near the SH3 domain of Toca-1 and FBP17 positioned the N-WASP–WIP to be spatially close to the membrane for activation of actin polymerization. Therefore, curvature-dependent actin polymerization is stimulated by spatially appropriate interactions of EFC/F-BAR proteins and the N-WASP–WIP complex with the membrane.
Keywords:
- actin polymerization,
- EFC domain,
- F-BAR domain,
- membrane deformation,
- N-WASP-WIP complex
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