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The vasodilator‐stimulated phosphoprotein promotes actin polymerisation through direct binding to monomeric actin
Author(s) -
Walders-Harbeck Birgit,
Khaitlina Sofia Y,
Hinssen Horst,
Jockusch Brigitte M,
Illenberger Susanne
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)03356-2
Subject(s) - actin binding protein , phosphoprotein , actin , microbiology and biotechnology , actin remodeling , chemistry , mdia1 , actin cytoskeleton , phosphorylation , biophysics , biology , biochemistry , cytoskeleton , cell
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.