Control of high affinity interactions in the talin C terminus: how talin domains coordinate protein dynamics in cell adhesions.

2.50
Hdl Handle:
http://hdl.handle.net/10033/84767
Title:
Control of high affinity interactions in the talin C terminus: how talin domains coordinate protein dynamics in cell adhesions.
Authors:
Himmel, Mirko; Ritter, Anett; Rothemund, Sven; Pauling, Björg V; Rottner, Klemens; Gingras, Alexandre R; Ziegler, Wolfgang H
Abstract:
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.
Affiliation:
Interdisciplinary Centre for Clinical Research (IZKF) Leipzig, Faculty of Medicine, University of Leipzig, D-04103 Leipzig, Germany.
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.
Journal:
The Journal of biological chemistry
Issue Date:
15-May-2009
URI:
http://hdl.handle.net/10033/84767
DOI:
10.1074/jbc.M900266200
PubMed ID:
19278997
Type:
Article
Language:
en
ISSN:
0021-9258
Appears in Collections:
Publications of RG Cytoskeleton Dynamics (CYD)

Full metadata record

DC FieldValue Language
dc.contributor.authorHimmel, Mirkoen
dc.contributor.authorRitter, Anetten
dc.contributor.authorRothemund, Svenen
dc.contributor.authorPauling, Björg Ven
dc.contributor.authorRottner, Klemensen
dc.contributor.authorGingras, Alexandre Ren
dc.contributor.authorZiegler, Wolfgang Hen
dc.date.accessioned2009-10-23T14:02:31Z-
dc.date.available2009-10-23T14:02:31Z-
dc.date.issued2009-05-15-
dc.identifier.citationControl 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.en
dc.identifier.issn0021-9258-
dc.identifier.pmid19278997-
dc.identifier.doi10.1074/jbc.M900266200-
dc.identifier.urihttp://hdl.handle.net/10033/84767-
dc.description.abstractIn 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.en
dc.language.isoenen
dc.subject.meshActinsen
dc.subject.meshAnimalsen
dc.subject.meshBinding Sitesen
dc.subject.meshCell Adhesionen
dc.subject.meshCell Lineen
dc.subject.meshCytoskeletonen
dc.subject.meshFocal Adhesionsen
dc.subject.meshIntegrinsen
dc.subject.meshMiceen
dc.subject.meshModels, Biologicalen
dc.subject.meshProtein Structure, Secondaryen
dc.subject.meshProtein Structure, Tertiaryen
dc.subject.meshTalinen
dc.titleControl of high affinity interactions in the talin C terminus: how talin domains coordinate protein dynamics in cell adhesions.en
dc.typeArticleen
dc.contributor.departmentInterdisciplinary Centre for Clinical Research (IZKF) Leipzig, Faculty of Medicine, University of Leipzig, D-04103 Leipzig, Germany.en
dc.identifier.journalThe Journal of biological chemistryen

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