Control of high affinity interactions in the talin C terminus: how talin domains coordinate protein dynamics in cell adhesions.
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Authors
Himmel, MirkoRitter, Anett
Rothemund, Sven
Pauling, Björg V
Rottner, Klemens
Gingras, Alexandre R
Ziegler, Wolfgang H
Issue Date
2009-05-15
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Show full item recordAbstract
In cell-extracellular matrix junctions (focal adhesions), the cytoskeletal protein talin is central to the connection of integrins to the actin cytoskeleton. Talin is thought to mediate this connection via its two integrin, (at least) three actin, and several vinculin binding sites. The binding sites are cryptic in the head-to-rod autoinhibited cytoplasmic form of the protein and require (stepwise) conformational activation. This activation process, however, remains poorly understood, and there are contradictory models with respect to the determinants of adhesion site localization. Here, we report turnover rates and protein-protein interactions in a range of talin rod domain constructs varying in helix bundle structure. We conclude that several bundles of the C terminus cooperate to regulate targeting and concomitantly tailor high affinity interactions of the talin rod in cell adhesions. Intrinsic control of ligand binding activities is essential for the coordination of adhesion site function of talin.Citation
Control of high affinity interactions in the talin C terminus: how talin domains coordinate protein dynamics in cell adhesions. 2009, 284 (20):13832-42 J. Biol. Chem.Affiliation
Interdisciplinary Centre for Clinical Research (IZKF) Leipzig, Faculty of Medicine, University of Leipzig, D-04103 Leipzig, Germany.PubMed ID
19278997Type
ArticleLanguage
enISSN
0021-9258ae974a485f413a2113503eed53cd6c53
10.1074/jbc.M900266200
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