PMID: 11341949May 9, 2001Paper

Mutual effects of alpha-actinin, calponin and filamin on actin binding

Biochimica Et Biophysica Acta
O O Panasenko, N B Gusev

Abstract

The mutual effect of three actin-binding proteins (alpha-actinin, calponin and filamin) on the binding to actin was analyzed by means of differential centrifugation and electron microscopy. In the absence of actin alpha-actinin, calponin and filamin do not interact with each other. Calponin and filamin do not interfere with each other in the binding to actin bundles. Slight interference was observed in the binding of alpha-actinin and calponin to actin bundles. Higher ability of calponin to depress alpha-actinin binding can be due to the higher stoichiometry calponin/actin in the complexes formed. The largest interference was observed in the pair filamin-alpha-actinin. These proteins interfere with each other in the binding to the bundled actin filaments; however, neither of them completely displaced another protein from its complexes with actin. The structure of actin bundles formed in the presence of any one actin-binding protein was different from that observed in the presence of binary mixtures of two actin-binding proteins. In the case of calponin or its binary mixtures with alpha-actinin or filamin the total stoichiometry actin-binding protein/actin was larger than 0.5. This means that alpha-actinin, calponin and filamin ...Continue Reading

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Citations

Aug 2, 2012·Biochimica Et Biophysica Acta·Lucía Méndez-LópezJ Antonio Villamarín
Oct 6, 2005·Journal of Muscle Research and Cell Motility·Olesya V BukachNikolai B Gusev

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