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• W2013809269 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." @default.
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• W2013809269 date "2002-09-17" @default.
• W2013809269 modified "2023-09-26" @default.
• W2013809269 title "The vasodilator-stimulated phosphoprotein promotes actin polymerisation through direct binding to monomeric actin" @default.
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• W2013809269 doi "https://doi.org/10.1016/s0014-5793(02)03356-2" @default.
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