血管舒张刺激磷蛋白VASP的肌动蛋白结合特性的表征

Characterization of the actin binding properties of the vasodilator-stimulated phosphoprotein VASP.

作者信息

Hüttelmaier S, Harbeck B, Steffens O, Messerschmidt T, Illenberger S, Jockusch B M

机构信息

Cell Biology, Zoological Institute, Technical University of Braunschweig, Germany.

出版信息

FEBS Lett. 1999 May 14;451(1):68-74. doi: 10.1016/s0014-5793(99)00546-3.

DOI:10.1016/s0014-5793(99)00546-3

PMID:10356985

Abstract

The vasodilator-stimulated phosphoprotein (VASP) colocalizes with the ends of stress fibers in cell-matrix and cell-cell contacts. We report here that bacterially expressed murine VASP directly interacts with skeletal muscle actin in several test systems including cosedimentation, viscometry and polymerization assays. It nucleates actin polymerization and tightly bundles actin filaments. The interaction with actin is salt-sensitive, indicating that the complex formation is primarily based on electrostatic interactions. Actin binding is confined to the C-terminal domain of VASP (EVH2). This domain, when expressed as a fusion protein with EGFP, associates with stress fibers in transiently transfected cells.

摘要

血管舒张刺激磷蛋白（VASP）在细胞与基质及细胞间接触部位与应力纤维末端共定位。我们在此报告，在包括沉降分析、粘度测定和聚合分析在内的多个测试系统中，细菌表达的小鼠VASP与骨骼肌肌动蛋白直接相互作用。它能引发肌动蛋白聚合并紧密捆绑肌动蛋白丝。与肌动蛋白的相互作用对盐敏感，表明复合物的形成主要基于静电相互作用。肌动蛋白结合局限于VASP的C末端结构域（EVH2）。当该结构域与EGFP作为融合蛋白表达时，它会与瞬时转染细胞中的应力纤维结合。