p130 Cas (Crk-associated substrate (CAS), breast cancer antiestrogen resistance 1 (BCAR1)) is a docking protein containing multiple protein-protein interaction domains. The N-terminal SH3 domain functions as a molecular switch regulating CAS tyrosine phosphorylation, as it interacts with tyrosine kinases and phosphatases. The C-terminal Src binding domain contains a proline-rich motif that mediates interaction with the SH3 domains of Src-family kinases (SFKs). Phosphorylation of this domain at Tyr-762 in rat (Tyr-668 in mouse) promotes this interaction. The p130 Cas central substrate domain is characterized by 15 tyrosines present in Tyr-X-X-Pro (YXXP) motifs, including Tyr-165, Tyr-249, and Tyr-410. When phosphorylated, most YXXP motifs are able to serve as docking sites for proteins with SH2 or PTB domains. In addition, phosphorylation of Tyr-751 (Tyr-653 in human) near the C-terminal caspase recognition site can attenuate caspase cleavage, while dephosphorylation occurs during apoptosis and may facilitate p130 Cas degradation.
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Pellicena, P. & Miller, W.T. (2001) J Biol Chem. 276 (30):28190.
Nakamoto, T. et al. (1996) J Biol Chem. 271(15):8959.
*For more information, see UniProt Accession Q63767
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*All molecular weights (MW) are confirmed by comparison to Bio-Rad Rainbow Markers and to western blot mobilities of known proteins with similar MW.
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