Interaction of iodinated vinculin, metavinculin and alpha-actinin with cytoskeletal proteins

FEBS Lett. 1987 Aug 17;220(2):291-4. doi: 10.1016/0014-5793(87)80832-3.


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.

MeSH terms

  • Actinin / metabolism
  • Actins / metabolism*
  • Cell Membrane / metabolism
  • Cytoskeletal Proteins / metabolism*
  • Fibronectins / metabolism
  • Humans
  • In Vitro Techniques
  • Molecular Weight
  • Muscle Proteins / metabolism*
  • Protein Binding
  • Talin
  • Vinculin


  • Actins
  • Cytoskeletal Proteins
  • Fibronectins
  • Muscle Proteins
  • Talin
  • Actinin
  • Vinculin