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Structure of the PTB domain of tensin1 and a model for its recruitment to fibrillar adhesions.

ABSTRACT: Tensin is a cytoskeletal protein that links integrins to the actin cytoskeleton at sites of cell-matrix adhesion. Here we describe the crystal structure of the phosphotyrosine-binding (PTB) domain of tensin1, and show that it binds integrins in an NPxY-dependent fashion. Alanine mutagenesis of both the PTB domain and integrin tails supports a model of integrin binding similar to that of the PTB-like domain of talin. However, we also show that phosphorylation of the NPxY tyrosine, which disrupts talin binding, has a negligible effect on tensin binding. This suggests that tyrosine phosphorylation of integrin, which occurs during the maturation of focal adhesions, could act as a switch to promote the migration of tensin-integrin complexes into fibronectin-mediated fibrillar adhesions.

SUBMITTER: McCleverty CJ

PROVIDER: S-EPMC2206669 | biostudies-literature | 2007 Jun

REPOSITORIES: biostudies-literature

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Structure of the PTB domain of tensin1 and a model for its recruitment to fibrillar adhesions.

McCleverty Clare J CJ Lin Diane C DC Liddington Robert C RC

Protein science : a publication of the Protein Society 20070501 6

Tensin is a cytoskeletal protein that links integrins to the actin cytoskeleton at sites of cell-matrix adhesion. Here we describe the crystal structure of the phosphotyrosine-binding (PTB) domain of tensin1, and show that it binds integrins in an NPxY-dependent fashion. Alanine mutagenesis of both the PTB domain and integrin tails supports a model of integrin binding similar to that of the PTB-like domain of talin. However, we also show that phosphorylation of the NPxY tyrosine, which disrupts ...[more]

PMID: 17473008

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