Doing (F/L)PPPPs: EVH1 domains and their proline-rich partners in cell polarity and migration

被引：86

作者：

Renfranz, PJ

Beckerle, MC

机构：

[1] Univ Utah, Dept Biol, Salt Lake City, UT 84112 USA

[2] Univ Utah, Huntsman Canc Inst, Salt Lake City, UT 84112 USA

来源：

CURRENT OPINION IN CELL BIOLOGY | 2002年 / 14卷 / 01期

基金：

美国国家卫生研究院;

关键词：

D O I：

10.1016/S0955-0674(01)00299-X

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

Actin filament assembly is a tightly regulated process that functions in many aspects of cell physiology. Members of the Ena/VASP (Drosophila Enabled/vasodilator-stimulated phosphoprotein) family are key players in regulating actin filament assembly, in many cases through their association with binding partners that display a particular proline-rich motif, FPPPP. Ena/VASP proteins interact with these partners via the highly conserved EnaVASP homology 1 (EVH1) domain. The diverse array of binding partners for EVH1 domains, including cytoskeletal proteins such as zyxin, transmembrane guidance receptors such as Roundabout, and the T-cell signaling protein Fyb/SLAP, shows that these interactions are likely to be important in a number of cellular processes that require regulated actin filament assembly.

引用

页码：88 / 103

页数：16

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