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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Blockade of v-Src- stimulated tumor formation by the Src homology 3 domain of Crk-associated substrate (Cas).

Crk-associated substrate (Cas) is highly phosphorylated by v-Src and plays a critical role in v-Src-induced cell transformation. In this study, we found that the Src homology (SH) 3 domain of Cas blocked v-Src-stimulated anchorage-independent cell growth, Matrigel invasion, and tumor growth in nude mice. Biochemical analysis revealed that the Cas SH3 domain selectively inhibited v-Src- stimulated activations of AKT and JNK, but not ERK and STAT3. Attenuation of the AKT pathway by the Cas SH3 domain rendered v-Src-transformed cells susceptible to apoptosis. Inhibition of the JNK pathway by the Cas SH3 domain led to suppression of v-Src-stimulated invasion. Taken together, our results indicate that the Cas SH3 domain has an anti-tumor function, which severely impairs the transforming potential of v-Src.[1]

References

  1. Blockade of v-Src-stimulated tumor formation by the Src homology 3 domain of Crk-associated substrate (Cas). Cheng, C.H., Yu, K.C., Chen, H.L., Chen, S.Y., Huang, C.H., Chan, P.C., Wung, C.W., Chen, H.C. FEBS Lett. (2004) [Pubmed]
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