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|標題:||Blockade of v-Src-stimulated tumor formation by the Src homology 3 domain of Crk-associated substrate (Cas)||作者:||Cheng, C.H.
|關鍵字:||Src;Crk-associated substrate;Src homology 3 domain;tumor;anoikis;invasion;focal adhesion kinase;cell-migration;induced apoptosis;tyrosine;kinase;direct binding;p130(cas);protein;transformation;survival;growth||Project:||Febs Letters||期刊/報告no：:||Febs Letters, Volume 557, Issue 1-3, Page(s) 221-227.||摘要:||
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. (C) 2003 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
|Appears in Collections:||生命科學院|
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