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Intramolecular interactions in vinculin control α‐actinin binding to the vinculin head
Author(s) -
Kroemker Martina,
Rüdiger Angelika-H.,
Jockusch Brigitte M.,
Rüdiger Manfred
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)01216-4
Subject(s) - vinculin , chemistry , binding site , microbiology and biotechnology , biophysics , biochemistry , biology , cytoskeleton , cell
Using blot overlay techniques we have investigated the interaction of vinculin with α‐actinin. We show that an α‐actinin binding site is located in the 90 kDa vinculin head and confirm a vinculin binding site in the C‐terminal rod of α‐actinin, as recently reported by McGregor et al. [(1994) Biochem. J. 310, 225–233]. The isolated vinculin head binds much more strongly to α‐actinin than intact vinculin. Using a proteolytic 81 kDa head fragment, we show that vinculin residues 1–107 are required for α‐actinin binding. Antibodies directed against vinculin residues 808–850 inhibit the vinculin‐α‐actinin binding, suggesting that this sequence is directly involved in, or topographically related to, the α‐actinin binding site.