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

Abstract:

: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 Ena/VASP 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.

journal_name

Curr Opin Cell Biol

authors

Renfranz PJ,Beckerle MC

doi

10.1016/s0955-0674(01)00299-x

subject

Has Abstract

pub_date

2002-02-01 00:00:00

pages

88-103

issue

1

eissn

0955-0674

issn

1879-0410

pii

S095506740100299X

journal_volume

14

pub_type

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