Bar domain proteins: a role in tubulation, scission and actin assembly in clathrin-mediated endocytosis

被引：176

作者：

Dawson, John C. ^{[1
]}

Legg, John A. ^{[1
]}

Machesky, Laura M. ^{[1
]}

机构：

[1] Univ Birmingham, Sch Biosci, Birmingham B15 2TT, W Midlands, England

来源：

TRENDS IN CELL BIOLOGY | 2006年 / 16卷 / 10期

基金：

英国医学研究理事会;

关键词：

D O I：

10.1016/j.tcb.2006.08.004

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

Endocytosis is an important way for cells to take up liquids and particles from their environment. It requires membrane bending to be coupled with membrane fission, and the actin cytoskeleton has an active role in membrane remodelling. Here, we review recent research into the function of Bin-Amphiphysin-Rvs (BAR) domain proteins, which can sense membrane curvature and recruit actin to membranes. BAR proteins interact with the endocytic and cytoskeletal machinery, including the GTPase dynamin (which mediates vesicle fission), N-WASP (an Arp2/3 complex regulator) and synaptojanin (a phosphoinositide phosphatase). We describe three classes of BAR domains, BAR, N-BAR and F-BAR, providing examples of each discussing and how they function in linking membranes to the actin cytoskeleton in endocytosis.

引用

页码：493 / 498

页数：6

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