Intramolecular interactions in vinculin control alpha-actinin binding to the vinculin head

FEBS Lett. 1994 Dec 5;355(3):259-62. doi: 10.1016/0014-5793(94)01216-4.

Abstract

Using blot overlay techniques we have investigated the interaction of vinculin with alpha-actinin. We show that an alpha-actinin binding site is located in the 90 kDa vinculin head and confirm a vinculin binding site in the C-terminal rod of alpha-actinin, as recently reported by McGregor et al. [(1994) Biochem. J. 310, 225-233]. The isolated vinculin head binds much more strongly to alpha-actinin than intact vinculin. Using a proteolytic 81 kDa head fragment, we show that vinculin residues 1-107 are required for alpha-actinin binding. Antibodies directed against vinculin residues 808-850 inhibit the vinculin-alpha-actinin binding, suggesting that this sequence is directly involved in, or topographically related to, the alpha-actinin binding site.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actinin / metabolism*
  • Binding Sites
  • Electrophoresis, Polyacrylamide Gel
  • Ligands
  • Mass Spectrometry
  • Models, Structural
  • Molecular Probes
  • Protein Binding
  • Vinculin / metabolism*

Substances

  • Ligands
  • Molecular Probes
  • Actinin
  • Vinculin