Evidence for direct binding of vinculin to actin filaments

FEBS Letters

Ruhnau, Klaus¹  Wegner, Albrecht¹ 

[1]Institute of Physiological Chemistry, Ruhr-University Bochum, PO Box 102148, D-4630 Bochum, FRG

关键词: Actin;    Vinculin;    Tropomyosin;    Staining;    Fluorescence;   

DOI  :  10.1016/0014-5793(88)80595-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The interaction of vinculin with actin filaments was investigated by methods which exclude interference by contaminating proteins which may occur in vinculin preparations. Vinculin which was blotted from SDS-polyacrylamide gels onto nitrocellulose, was stained specifically by fluorescently labeled polymeric actin (100 mM KCl, 2 mM MgCl₂). Vinculin which was purified from α-actinin and an actin polymerization-inhibiting protein (HA1), was found to be cosedimented with polymeric actin. Maximally one vinculin molecule was cosedimented per one hundred actin filament subunits. Half maximal binding of vinculin was observed at about 0.25 μM free vinculin. Vinculin could be replaced from actin by the addition of tropomyosin.

【 授权许可】

Unknown