0000000000419880

AUTHOR

Sabine Wilhelm

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Differential VASP phosphorylation controls remodeling of the actin cytoskeleton

2009

Proteins of the Enabled/vasodilator-stimulated phosphoprotein (Ena/VASP) family link signal transduction pathways to actin cytoskeleton dynamics. VASP is substrate of cAMP-dependent, cGMP-dependent and AMP-activated protein kinases that primarily phosphorylate the sites S157, S239 and T278, respectively. Here, we systematically analyzed functions of VASP phosphorylation patterns for actin assembly and subcellular targeting in vivo and compared the phosphorylation effects of Ena/VASP family members. Methods used were the reconstitution of VASP-null cells with `locked' phosphomimetic VASP mutants, actin polymerization of VASP mutants in vitro and in living cells, site-specific kinase-mediated…

macromolecular substancesBiologyCell LineMiceAnimalsHumansPhosphorylationCytoskeletonCytoskeletonActinMice KnockoutKinaseMicrofilament ProteinsEna/Vasp homology proteinsActin remodelingCell BiologyPhosphoproteinsActin cytoskeletonActinsCell biologyMice Inbred C57BLProtein TransportPhosphoproteinPhosphorylationCell Adhesion MoleculesResearch ArticleJournal of Cell Science
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