期刊
PROTEIN SCIENCE
卷 16, 期 6, 页码 1223-1229出版社
WILEY
DOI: 10.1110/ps.072798707
关键词
structure/function studies; crystallography; calorimetry; mutagenesis (site-directed and general); docking proteins; surface plasmon resonance
资金
- NIGMS NIH HHS [GM22289] Funding Source: Medline
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.
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