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Title: The cytoskeletal protein talin contains at least two distinct vinculin binding domains.
Authors: Gilmore, A. P.
Wood, C.
Ohanian, V.
Jackson, P.
Patel, B.
Rees, D. J.
Hynes, R. O.
Critchley, D. R.
First Published: 15-Jul-1993
Publisher: Rockefeller University Press
Citation: Journal of Cell Biology, 1993, 122 (2), pp. 337-347
Abstract: We have mapped the vinculin-binding sites in the cytoskeletal protein talin as well as those sequences which target the talin molecule to focal contacts. Using a series of overlapping talin-fusion proteins expressed in E. coli and 125I-vinculin in both gel-overlay and microtitre well binding assays, we present evidence for three separable binding sites for vinculin. All three are in the tail segment of talin (residues 434-2541) and are recognized by the same fragment of vinculin (residues 1-258). Two sites are adjacent to each other and span residues 498-950, and the third site is more than 700 residues distant in the primary sequence. Scatchard analysis of 125I-vinculin binding to talin also indicates three sites, each with a similar affinity (Kd = 2-6 x 10(-7) M). We also detect a substoichiometric interaction of higher affinity (Kd = 3 x 10(-8) M) which remains unexplained. By expressing regions of the chicken talin molecule in heterologous cells, we have shown that the sequences required to target talin to focal contacts overlap those which bind vinculin.
DOI Link: 10.1083/jcb.122.2.337
ISSN: 0021-9525
Version: Publisher Version
Status: Peer-reviewed
Type: Journal Article
Rights: © 1993 Rockefeller University Press CC BY-NC-SA
Appears in Collections:Published Articles, Dept. of Molecular and Cell Biology

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