Interaction of iodinated vinculin, metavinculin and alpha-actinin with cytoskeletal proteins.
Iodinated vinculin, metavinculin and alpha-actinin were used to probe the interaction of these proteins with electrophoretically separated cytoskeletal proteins. Using the gel overlay technique, we detected strong binding of 125I-vinculin and 125I-metavinculin to alpha-actinin, 175 kDa polypeptide, talin, vinculin and metavinculin themselves, and moderate binding to actin. 125I-alpha-actinin was capable of interacting with vinculin and metavinculin. The specific binding of 125-I-alpha-actinin to vinculin and metavinculin immobilized on a polysterene surface was also demonstrated. We suggest that the ability of vinculin and alpha-actinin to form a complex may be realized in microfilament-membrane linkages.
D000185:Actinin / Q000378:metabolism; D000199:Actins / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism; D003598:Cytoskeletal Proteins / Q000378:metabolism*; D005353:Fibronectins / Q000378:metabolism; D006801:Humans; D066298:In Vitro Techniques; D008970:Molecular Weight; D009124:Muscle Proteins / Q000378:metabolism*; D011485:Protein Binding; D016608:Talin; D016596:Vinculin
D000199:Actins; D003598:Cytoskeletal Proteins; D005353:Fibronectins; D009124:Muscle Proteins; D016608:Talin; D000185:Actinin; D016596:Vinculin