title: 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.
authors.affiliation: Department of Biology and Huntsman Cancer Institute, 2000 East Circle of Hope, University of Utah, Salt Lake City, UT 84112-5550, USA.
authors.forename: Patricia J
authors.initials: PJ
authors.lastname: Renfranz
authors.forename: Mary C
authors.initials: MC
authors.lastname: Beckerle
mesh_terms: D020816:Amino Acid Motifs; D000818:Animals; D015815:Cell Adhesion Molecules / Q000737:chemistry / Q000378:metabolism / Q000502:physiology; D002465:Cell Movement; D016764:Cell Polarity; D004848:Epithelium / Q000254:growth & development; D008840:Microfilament Proteins / Q000737:chemistry* / Q000378:metabolism / Q000502:physiology*; D008954:Models, Biological; D008958:Models, Molecular; D010750:Phosphoproteins / Q000737:chemistry / Q000378:metabolism / Q000502:physiology; D011392:Proline / Q000378:metabolism; D017434:Protein Structure, Tertiary; D000098662:Vasodilator-Stimulated Phosphoprotein
chemical_list: D015815:Cell Adhesion Molecules; D008840:Microfilament Proteins; D010750:Phosphoproteins; D000098662:Vasodilator-Stimulated Phosphoprotein; D011392:Proline