Phosphorylation of BCAR1 by SRC-PTK2 complex

Stable Identifier
Reaction [transition]
Homo sapiens
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SH3-mediated binding of BCAR1/p130Cas to PTK2 is linked to enhanced tyrosine phosphorylation of BCAR1 at multiple sites. The Cas substrate domain contains 15 separate YxxP motifs, a main site of tyrosine phosphorylation on the BCAR1 molecule. Once phosphorylated, this domain serves as a docking site for the SH2 domains of CRK or NCK adaptor proteins that affect the downstream MAPK signalling pathway, resulting in cell survival and increased motility.
Literature References
PubMed ID Title Journal Year
8621540 Direct binding of C-terminal region of p130Cas to SH2 and SH3 domains of Src kinase

Yazaki, Y, Sakai, R, Ozawa, K, Hirai, H, Nakamoto, T

J. Biol. Chem. 1996
16581250 p130Cas: a versatile scaffold in signaling networks

Defilippi, P, Di Stefano, P, Cabodi, S

Trends Cell Biol 2006
12585966 Bidirectional integrin alphaIIbbeta3 signalling regulating platelet adhesion under flow: contribution of protein kinase C

Giuliano, S, Jackson, SP, Rooney, M, Nesbitt, WS

Biochem J 2003
12640026 Focal adhesion kinase: the first ten years

Parsons, JT

J Cell Sci 2003
Catalyst Activity

protein tyrosine kinase activity of BCAR1:Talin:RIAM:ECM ligands:alphaIIb beta3:p-Y419 SRC:p-6Y-PTK2 [plasma membrane]

Orthologous Events
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