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Casting light on focal adhesions

Nature Genetics volume 19, pages 309–311 (1998)Cite this article

Cas and focal adhesions

Cas is phosphorylated on multiple tyrosine residuces following attachment of cells to ECM proteins like fibronectin5,6; its phosphorylation is critical to its capacity to organize FA protein-signalling complexes. The protein tyrosine kinase FAK is thought to phosphorylate the Y-D-Y-V motif on Cas, which, in turn, binds to Src family kinase SH2 domains. Src kinase then reciprocates, in a sense, by phosphorylating the multiple Y-X-X-P motifs on Cas which serve as binding sites for the adapter protein Crk, which, in turn, binds multiple cellular proteins through its SH3 domains7. Phosphorylation thus allows Cas to couple with multiple signalling pathways through the Crk adaptor.

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Figure 1: Focal adhesions and stress fibers in a cell attached to extracellular matrix.
Figure 2: Cas-binding interactions.

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  1. Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, 02115, Massachusetts, USA

    Joan S Brugge

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Brugge, J. Casting light on focal adhesions. Nat Genet 19, 309–311 (1998). https://doi.org/10.1038/1189

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