Interaction of alpha-actinin and vinculin with actin: opposite effects on filament network formation. | Zendy

B. M. Jockusch | Zendy; G. Isenberg | Zendy

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Interaction of alpha-actinin and vinculin with actin: opposite effects on filament network formation.

Author(s) -

B. M. Jockusch,

G. Isenberg

Publication year - 1981

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.78.5.3005

Subject(s) - vinculin , actinin , actin , actin binding protein , biophysics , protein filament , microbiology and biotechnology , chemistry , actin remodeling , actina , cytoskeleton , actin cytoskeleton , biology , biochemistry , cell

The interaction of actin filaments with two actin-associated proteins, alpha-actinin and vinculin (Mr 130,000 protein), was studied in vitro with viscometry and light and electron microscopy. Vinculin, like alpha-actinin, binds to F-actin, and the two proteins were found to 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, whereas vinculin forms actin bundles that display a paracrystalline substructure. In viscometric assays, alpha-actinin mimics the effect of actin gelation factors, whereas vinculin acts as a gelation inhibitor. These findings imply complementary functions of these proteins in the regulation of cellular mobility.

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