The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Src kinase activation by direct interaction with the integrin β cytoplasmic domain
Open accessAbstract
Src tyrosine kinases transmit integrin-dependent signals pivotal for cell movement and proliferation. Here, we establish a mechanism for Src activation by integrins. c-Src is shown to bind constitutively and selectively to β3 integrins through an interaction involving the c-Src SH3 domain and the carboxyl-terminal region of the β3 cytoplasmic tail. Clustering of β3 integrins in vivo activates c-Src and induces phosphorylation of Tyr-418 in the c-Src activation loop, a reaction essential for adhesion-dependent phosphorylation of Syk, a c-Src substrate. Unlike c-Src, Hck, Lyn, and c-Yes bind more generally to β1A, β2, and β3 cytoplasmic tails. These results invoke a model whereby Src is primed for activation by direct interaction with an integrin β tail, and integrin clustering stabilizes activated Src by inducing intermolecular autophosphorylation. The data provide a paradigm for integrin regulation of Src and a molecular basis for the similar functional defects of osteoclasts or platelets from mice lacking β3 integrins or c-Src.
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Calderwood, D. A., Zent, R., Grant, R., Rees, D. J. G., Hynes, R. O., & Ginsberg, M. H. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.40.28071 · Cited by 720
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Metadata
- Authors
- Arias-Salgado, E. G., Lizano, S., Sarkar, S., Brugge, J. S., Ginsberg, M. H., & Shattil, S. J.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2003-10-30
- Volume
- 100
- Issue
- 23
- Pages
- 13298-13302
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2003698382
- Cited by
- 554
- References
- 2
- FWCI
- 16.23
- Type
- journal article
- Language
- en
- Open access
- green
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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