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    FEBS Lett. 2002 Oct 9;529(2-3):275-80.

    The vasodilator-stimulated phosphoprotein promotes actin polymerisation through direct binding to monomeric actin.

    Walders-Harbeck B, Khaitlina SY, Hinssen H, Jockusch BM, Illenberger S.

    Source

    Cell Biology, Zoological Institute, Technical University of Braunschweig, Biocenter, Spielmannstrasse 7, D-38092 Braunschweig, Germany.

    Abstract

    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.

    PMID:
    12372613
    [PubMed - indexed for MEDLINE]

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