Control of High Affinity Interactions in the Talin C Terminus: HOW TALIN DOMAINS COORDINATE PROTEIN DYNAMICS IN CELL ADHESIONS*S⃞
AUTOR(ES)
Himmel, Mirko
FONTE
American Society for Biochemistry and Molecular Biology
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2679484Documentos Relacionados
- Optimizing pH Response of Affinity between Protein G and IgG Fc: HOW ELECTROSTATIC MODULATIONS AFFECT PROTEIN-PROTEIN INTERACTIONS*S⃞
- STAT3-Stathmin Interactions Control Microtubule Dynamics in Migrating T-cells*S⃞
- Human tyrosinase-like protein (TYRL) carboxy terminus: closer homology with the mouse protein than previously reported
- Single Terminus, Double Control♦: The C Terminus of Na+,K+-ATPase Controls Na+ Affinity on Both Sides of the Membrane through Arg935
- Structure of the Tyrosine-sulfated C5a Receptor N Terminus in Complex with Chemotaxis Inhibitory Protein of Staphylococcus aureus*S⃞