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

FEBS Letters

Walders-Harbeck, Birgit¹  Hinssen, Horst³  Illenberger, Susanne¹  Jockusch, Brigitte M¹  Khaitlina, Sofia Y² 

[1] Cell Biology, Zoological Institute, Technical University of Braunschweig, Biocenter, Spielmannstr. 7, D-38092 Braunschweig, Germany;Institute of Cytology, Russian Academy of Sciences, 194064 St. Petersburg, Russia;Department of Biochemical Cell Biology, University of Bielefeld, D-33501 Bielefeld, Germany

关键词: Actin dynamics;    Ena/Mena/vasodilator-stimulated phosphoprotein;    G-actin;    Nucleation;    Polymerisation;    VASP;    vasodilator-stimulated phosphoprotein;    EVH;    Ena/VASP homology domain;    BiPro;    birch profilin;    ECP;    Escherichia coli protease;   

DOI  :  10.1016/S0014-5793(02)03356-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown