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Background
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CRK is a member of an adapter protein family that binds to several tyrosine-phosphorylated proteins. It has several SH2 and SH3 domains (src-homology domains) and is involved in several signaling pathways, recruiting cytoplasmic proteins in the vicinity of tyrosine kinase through SH2-phosphotyrosine interaction. The N-terminal SH2 domain of this protein functions as a positive regulator of transformation whereas the C-terminal SH3 domain functions as a negative regulator of transformation.
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Background
References
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- Bougneres, L., et al., J. Cell Biol. 166(2):225-235 (2004).
- Stoletov, K.V., et al., Exp. Cell Res. 295(1):258-268 (2004).
- Miller, C.T., et al., Oncogene 22(39):7950-7957 (2003).
- Sun, J., et al., J. Biol. Chem. 278(35):32794-32800 (2003).
- Zhang, X.A., et al., J. Biol. Chem. 278(29):27319-27328 (2003).
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