血管舒张刺激磷蛋白通过直接结合单体肌动蛋白来促进肌动蛋白聚合。
The vasodilator-stimulated phosphoprotein promotes actin polymerisation through direct binding to monomeric actin.
作者信息
Walders-Harbeck Birgit, Khaitlina Sofia Y, Hinssen Horst, Jockusch Brigitte M, Illenberger Susanne
机构信息
Cell Biology, Zoological Institute, Technical University of Braunschweig, Biocenter, Spielmannstrasse 7, D-38092 Braunschweig, Germany.
出版信息
FEBS Lett. 2002 Oct 9;529(2-3):275-80. doi: 10.1016/s0014-5793(02)03356-2.
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.
血管舒张刺激磷蛋白（VASP）作为肌动蛋白动力学的细胞调节剂发挥作用。VASP可能启动肌动蛋白聚合，这表明它与单体肌动蛋白存在直接相互作用。本研究表明，VASP直接与肌动蛋白单体结合，且复合物的形成取决于EVH2结构域中一个保守的四氨基酸基序。该基序内的点突变会大幅削弱VASP与肌动蛋白单体的相互作用，从而消除VASP的任何肌动蛋白成核活性。此外，发现肌动蛋白成核依赖于VASP的寡聚化，因为VASP单体无法诱导肌动蛋白丝的形成。磷酸化会对VASP与肌动蛋白单体的相互作用产生负面影响，从而阻止VASP诱导的肌动蛋白丝形成。
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