Talin is an important cytoskeletal component of integrin adhesion sites. Calpins cleave talin precursor (240 kDa) into an amino-terminal globular head domain of 47 kDa and a carboxyl-terminal 190 kDa rod domain. The talin head domain contains a FERM domain that binds integrins, PIP kinase (Type I), and FAK. The rod domain has several vinculin-binding sites, a second integrin-binding site, and two actin-binding sites. These talin protein-protein interactions are critical for integrin activation, focal adhesion formation, and cell migration. Talin regulation may occur through phosphorylation and regulated degradation. The talin head domain binds Smurf1, an E3 ubiquitin ligase, and this interaction leads to talin head ubiquitylation and degradation. Cdk5 can phosphorylate Ser-425 in the head domain, and this inhibits both binding to Smurf1 and subsequent degradation. The S425A talin mutant resists Cdk5 phosphorylation, increases susceptibility to Smurf1-mediated ubiquitylation, and inhibits cell migration. Thus, talin head phosphorylation may be important for regulating adhesion stability and cell migration.
Huang, C. et al. (2009) Nat Cell Biol. 11(5):624.
Moser, M. et al. (2009) Science. 324(5929):895.
Ratnikov, B. et al. (2005) J. Cell Sci. 118:4921.
*For more information, see UniProt Accession Q9Y490
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*All molecular weights (MW) are confirmed by comparison to Bio-Rad Rainbow Markers and to western blot mobilities of known proteins with similar MW.
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