Source

Rabbit

Reactivity

Human;Mouse;Rat

Background

p130 Cas is a docking protein containing multiple protein-protein interaction domains. The amino-terminal SH3 domain may function as a molecular switch regulating CAS tyrosine phosphorylation, as it interacts with focal adhesion kinase and the FAK-related kinase PYK2, as well as the tyrosine phosphatases PTP-1B and PTP-PEST. The carboxy-terminal Src binding domain contains a proline-rich motif that mediates interaction with the SH3 domains of Src-family kinases and a tyrosine phosphorylation site that can promote interaction with the SH2 domain of SFKs. The p130 Cas central substrate domain, the major region of tyrosine phosphorylation, is characterized by 15 tyrosines present in Tyr-X-X-Pro motifs, including Tyr165, 249, and 410. When phosphorylated, most YXXP motifs are able to serve as docking sites for proteins with SH2 or PTB domains including adaptors, C-Crk, Nck, and inositol 5'-phosphatase 2. The tyrosine phosphorylation of p130 Cas has been implicated as a key signaling step in integrin control of normal cellular behaviors including motility, proliferation, and survival. Aberrant Cas tyrosine phosphorylation may contribute to cell transformation by certain oncoproteins.

References

[1] Polte, T.R. and Hanks, S.K. (1997) J Biol Chem 272, 5501-9.
[2] Astier, A. et al. (1997) J Biol Chem 272, 228-32.
[3] Liu, F. et al. (1996) J Biol Chem 271, 31290-5.
[4] Garton, A.J. et al. (1997) Oncogene 15, 877-85.
[5] Ruest, P.J. et al. (2001) Mol Cell Biol 21, 7641-7652.
[6] Bouton, A.H. et al. (2001) Oncogene 20, 6448-6458.

Raw materials

Preparation Products