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Curr Opin Cell Biol. 2002 Feb;14(1):88-103.

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

Author information

1
Department of Biology and Huntsman Cancer Institute, 2000 East Circle of Hope, University of Utah, Salt Lake City, UT 84112-5550, USA.

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.

PMID:
11792550
DOI:
10.1016/s0955-0674(01)00299-x
[Indexed for MEDLINE]

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