Fak/Src phosphorylate p130Cas

Stable Identifier
Reaction [transition]
Mus musculus
SVG |   | PPTX  | SBGN
Fak/Src phosphorylate p130Cas

P130CAS (CRK-associated substrate/BCAR1) contains multiple protein-protein interaction domains including an N-terminal SH3 domain, an interior substrate domain (SD), a Src-binding domain (SBD) near the C-terminus and a conserved C-terminal Cas-family homology (CCH) domain. The SH3 and CCH domains mediate localization to focal adhesions (FAs) while SD and SBD are involved in initiating signaling events (Meenderink et al. 2010, Shin et al. 2004). The BCAR1 SD undergoes tyrosine phosphorylation and mediates signals by recruiting downstream effectors. The SD is characterised by fifteen YxxP motifs, of which ten can be efficiently phosphorylated by Src family kinases (SFKs) (Shin et al. 2004). PTK2/FAK kinase phosphorylates the nearby SBD tyrosines 664 and 666 (mouse 668/670). These SBD tyrosines provide the additional binding sites for Src-SH2 domains, stabilizing the SRC-BCAR1 association (Ruest et al. 2001). Note: Phosphorylated tyrosine numbering in human BCAR1 is based on similarity with the mouse p130Cas.

Literature References
PubMed ID Title Journal Year
11604500 Mechanisms of CAS substrate domain tyrosine phosphorylation by FAK and Src

Ruest, PJ, Shin, NY, Polte, TR, Zhang, X, Hanks, SK

Mol. Cell. Biol. 2001
15247284 Subsets of the major tyrosine phosphorylation sites in Crk-associated substrate (CAS) are sufficient to promote cell migration

Shin, NY, Dise, RS, Schneider-Mergener, J, Ritchie, MD, Kilkenny, DM, Hanks, SK

J. Biol. Chem. 2004
7479864 Interaction between focal adhesion kinase and Crk-associated tyrosine kinase substrate p130Cas

Polte, TR, Hanks, SK

Proc. Natl. Acad. Sci. U.S.A. 1995
Catalyst Activity
Catalyst Activity
protein tyrosine kinase activity of Fak1:p130Cas:Src [cytosol]
Physical Entity
Orthologous Events
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