Evidence for direct binding of vinculin to actin filaments
Authors:
- Albrecht WegnerAWAlbrecht Wegner
- 8 February 1988
- journal article
- Published by Wiley in FEBS Letters
- Vol. 228 (1) , 105-108
Abstract
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.Keywords
This publication has 27 references indexed in Scilit:
- Specific interaction of vinculin with α-actininBiochemical and Biophysical Research Communications, 1987
- A re-examination of the interaction of vinculin with actin.Journal of Cell Biology, 1986
- The lack of interaction between vinculin and actinCell Motility, 1986
- Isolation and partial characterization of human platelet vinculin.Journal of Cell Biology, 1985
- Detection of vinculin-binding proteins with an 125I-vinculin gel overlay technique.Journal of Cell Biology, 1983
- Structural aspects of vinculin-actin interactionsJournal of Molecular Biology, 1982
- High-affinity interaction of vinculin with actin filaments in vitroCell, 1982
- Equilibrium of the actin-tropomyosin interactionJournal of Molecular Biology, 1979
- Synthesis of a Protein‐Reactive ATP Analog and Its Application for the Affinity Labeling of Rabbit‐Muscle ActinEuropean Journal of Biochemistry, 1974
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970