Dynamin and the actin cytoskeleton cooperatively regulate plasma membrane invagination by BAR and F-BAR proteins

被引:491
作者
Itoh, T
Erdmann, KS
Roux, A
Habermann, B
Werner, H
De Camilli, P
机构
[1] Yale Univ, Sch Med, Dept Cell Biol, New Haven, CT 06510 USA
[2] Yale Univ, Sch Med, Howard Hughes Med Inst, Boyer Ctr Mol Med, New Haven, CT 06510 USA
[3] Scion Comp Innovat GmbH, Max Planck Inst Mol Cell Biol & Genet, D-01307 Dresden, Germany
关键词
D O I
10.1016/j.devcel.2005.11.005
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Cell membranes undergo continuous curvature changes as a result of membrane trafficking and cell motility. Deformations are achieved both by forces extrinsic to the membrane as well as by structural modifications in the bilayer or at the bilayer surface that favor the acquisition of curvature. We report here that a family of proteins previously implicated in the regulation of the actin cytoskeleton also have powerful lipid bilayer-deforming properties via an N-terminal module (F-BAR) similar to the BAR domain. Several such proteins, like a subset of BAR domain proteins, bind to dynamin, a GTPase implicated in endocytosis and actin dynamics, via SH3 domains. The ability of BAR and F-BAR domain proteins to induce tubular invaginations of the plasma membrane is enhanced by disruption of the actin cytoskeleton and is antagonized by dynamin. These results suggest a close interplay between the mechanisms that control actin dynamics and those that mediate plasma membrane invagination and fission.
引用
收藏
页码:791 / 804
页数:14
相关论文
共 79 条
[1]   Gapped BLAST and PSI-BLAST: a new generation of protein database search programs [J].
Altschul, SF ;
Madden, TL ;
Schaffer, AA ;
Zhang, JH ;
Zhang, Z ;
Miller, W ;
Lipman, DJ .
NUCLEIC ACIDS RESEARCH, 1997, 25 (17) :3389-3402
[2]   A Cdc42 target protein with homology to the non-kinase domain of FER has a potential role in regulating the actin cytoskeleton [J].
Aspenstrom, P .
CURRENT BIOLOGY, 1997, 7 (07) :479-487
[3]   N-WASP deficiency impairs EGF internalization and actin assembly at clathrin-coated pits [J].
Benesch, S ;
Polo, S ;
Lai, FPL ;
Anderson, KI ;
Stradal, TEB ;
Wehland, J ;
Rottner, K .
JOURNAL OF CELL SCIENCE, 2005, 118 (14) :3103-3115
[4]   Structure of the Sec23/24-Sar1 pre-budding complex of the COPII vesicle coat [J].
Bi, XP ;
Corpina, RA ;
Goldberg, J .
NATURE, 2002, 419 (6904) :271-277
[5]  
Bon E, 2000, YEAST, V16, P1229, DOI 10.1002/1097-0061(20000930)16:13<1229::AID-YEA618>3.0.CO
[6]  
2-Q
[7]   Myosin VI isoform localized to clathrin-coated vesicles with a role in clathrin-mediated endocytosis [J].
Buss, F ;
Arden, SD ;
Lindsay, M ;
Luzio, JP ;
Kendrick-Jones, J .
EMBO JOURNAL, 2001, 20 (14) :3676-3684
[8]   Differential distribution of dynamin isoforms in mammalian cells [J].
Cao, H ;
Garcia, F ;
McNiven, MA .
MOLECULAR BIOLOGY OF THE CELL, 1998, 9 (09) :2595-2609
[9]   The PCH family protein, Cdc15p, recruits two F-actin nucleation pathways to coordinate cytokinetic actin ring formation in Schizosaccharomyces pombe [J].
Carnahan, RH ;
Gould, KL .
JOURNAL OF CELL BIOLOGY, 2003, 162 (05) :851-862
[10]   Nervous wreck, an SH3 adaptor protein that interacts with Wsp, regulates synaptic growth in Drosophila [J].
Coyle, IP ;
Koh, YH ;
Lee, WCM ;
Slind, J ;
Fergestad, T ;
Littleton, JT ;
Ganetzky, B .
NEURON, 2004, 41 (04) :521-534