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Summary

Talin is a cytoskeletal component of integrin adhesion sites, cleaved into a 47 kDa head domain and a 190 kDa rod domain. The head domain binds integrins, PIP kinase, and FAK, while the rod domain has vinculin-binding sites, a second integrin-binding site, and actin-binding sites. Talin regulation occurs through phosphorylation and degradation, with the head domain binding Smurf1, an E3 ubiquitin ligase, leading to ubiquitylation and degradation. Phosphorylation of Ser-425 in the head domain by Cdk5 inhibits binding to Smurf1 and degradation. The S425A talin mutant resists Cdk5 phosphorylation, increasing susceptibility to Smurf1-mediated ubiquitylation and inhibiting cell migration.

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Talin is a cytoskeletal component of integrin adhesion sites, cleaved into a 47 kDa head domain and a 190 kDa rod domain.

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