Journal
FEBS LETTERS
Volume 529, Issue 2-3, Pages 275-280Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/S0014-5793(02)03356-2
Keywords
actin dynamics; Ena/Mena/vasodilator-stimulated phosphoprotein; G-actin; nucleation; polymerisation
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The vasodilator-stimulated phosphoprotein (VASP) functions as a cellular regulator of actin dynamics. VASP may initialise actin polymerisation, suggesting a direct interaction with monomeric actin. The present study demonstrates that VASP directly binds to actin monomers and that complex formation depends on a conserved four amino acid motif in the EVH2 domain. Point mutations within this motif drastically weaken VASP/G-actin interactions, thereby abolishing any actin-nucleating activity of VASP. Additionally, actin nucleation was found to depend on VASP oligomerisation since VASP monomers fail to induce the formation of actin filaments. Phosphorylation negatively affects VASP/G-actin interactions preventing VASP-induced actin filament formation. (C) 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
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