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Biochem Biophys Res Commun. 1987 Jul 31;146(2):554-60.

Specific interaction of vinculin with alpha-actinin.

Abstract

Vinculin and alpha-actinin are cytoskeletal proteins present at focal contacts of the ventral surface of cultured fibroblasts. We labelled alpha-actinin with an acceptor fluorophore and vinculin with a donor. A mixture of vinculin and alpha-actinin showed a 28% quench, due to energy transfer, suggesting an interaction. Quench of vinculin was dependent on the concentration of alpha-actinin; Scatchard analysis gives a dissociation constant in the microM range. Quench was inhibited by excess unlabelled alpha-actinin, and by reaction of the acceptor protein with p-chloromercuribenzoate. We found that vinculin had a slightly greater elution volume in a gel filtration column equilibrated with alpha-actinin, indicating a higher effective Stokes radius due to the interaction of the two proteins.

PMID:
3113423
DOI:
10.1016/0006-291x(87)90564-x
[Indexed for MEDLINE]

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