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Characterization of the actin binding properties of the vasodilator‐stimulated phosphoprotein VASP
Author(s) -
Hüttelmaier Stefan,
Harbeck Birgit,
Steffens Nils Ole,
Meßerschmidt Tania,
Illenberger Susanne,
Jockusch Brigitte M
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00546-3
Subject(s) - phosphoprotein , actin , actin binding protein , chemistry , microbiology and biotechnology , actin remodeling , transfection , biophysics , cytoskeleton , cell , actin cytoskeleton , biochemistry , biology , phosphorylation , gene
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.