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

被引：108

作者：

Hüttelmaier, S ^{[1
]}

Harbeck, B ^{[1
]}

Steffens, NO ^{[1
]}

Messerschmidt, T ^{[1
]}

Illenberger, S ^{[1
]}

Jockusch, BM ^{[1
]}

机构：

[1] Tech Univ Braunschweig, Inst Zool, D-38092 Braunschweig, Germany

来源：

FEBS LETTERS | 1999年 / 451卷 / 01期

关键词：

vasodilator-stimulated phosphoprotein; actin binding protein; focal contact; microfilament organization;

D O I：

10.1016/S0014-5793(99)00546-3

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

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. (C) 1999 Federation of European Biochemical Societies.

引用

页码：68 / 74

页数：7

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