Characterization of the actin binding properties of the vasodilator‐stimulated phosphoprotein VASP

FEBS Letters

Harbeck, Birgit¹  Steffens, Nils Ole¹  Meßerschmidt, Tania¹  Illenberger, Susanne¹  Hüttelmaier, Stefan¹  Jockusch, Brigitte M¹ 

[1] Cell Biology, Zoological Institute, Technical University of Braunschweig, Spielmannstr. 7, D-38092 Braunschweig, Germany

关键词: Vasodilator-stimulated phosphoprotein;    Actin binding protein;    Focal contact;    Microfilament organization;   

DOI  :  10.1016/S0014-5793(99)00546-3

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) 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.

【 授权许可】

Unknown