Interaction of alpha-actinin and vinculin with actin: opposite effects on filament network formation.
- 1 May 1981
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 78 (5) , 3005-3009
- https://doi.org/10.1073/pnas.78.5.3005
Abstract
The interaction of porcine skeletal muscle actin filaments with 2 actin-associated proteins, .alpha.-actinin and vinculin (Mr [molecular raho] 130,000 protein), was studied in vitro with viscometry and light microscopy and EM. Vinculin, like .alpha.-actinin, binds of F-actin. The 2 proteins have different effects on the formation of filament networks: .alpha.-actinin crosslinks individual filaments in a manner strongly dependent on temperature and acts as a spacer. Vinculin forms actin bundles that display a paracrystalline substructure. In viscometric assays, .alpha.-actinin mimics the effects of actin gelation factors and vinculin acts as a gelation inhibitor. Complementary functions of these proteins in the regulation of cellular mobility are implied.This publication has 24 references indexed in Scilit:
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