Focal adhesion kinase suppresses apoptosis by binding to the death domain of receptor-interacting protein

被引:149
作者
Kurenova, E
Xu, LH
Yang, XH
Baldwin, AS
Craven, RJ
Hanks, SK
Liu, ZG
Cance, WG
机构
[1] Univ Florida, Hlth Sci Ctr, Dept Surg, Gainesville, FL 32610 USA
[2] Univ Florida, Dept Biochem, Gainesville, FL 32610 USA
[3] Univ Florida, Dept Biol Mol, Gainesville, FL 32610 USA
[4] Univ N Carolina, Lineberger Comprehens Canc Ctr, Chapel Hill, NC 27599 USA
[5] Univ Kentucky, Dept Mol & Biomed Pharmacol, Lexington, KY 40536 USA
[6] Vanderbilt Univ, Sch Med, Dept Cell & Dev Biol, Nashville, TN 37232 USA
[7] NCI, Dept Cell & Canc Biol, Med Branch, Div Clin Sci,NIH, Bethesda, MD 20892 USA
关键词
D O I
10.1128/MCB.24.10.4361-4371.2004
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Tumor cells resist the apoptotic stimuli associated with invasion and metastasis by activating survival signals that suppress apoptosis. Focal adhesion kinase (FAK), a tyrosine kinase that is overexpressed in a variety of human tumors, mediates one of these survival signals. Attenuation of FAK expression in tumor cells results in apoptosis that is mediated by caspase 8- and FADD-dependent pathways, suggesting that death receptor pathways are involved in the process. Here, we report a functional link between FAK and death receptors. We have demonstrated that FAK binds to the death domain kinase receptor-interacting protein (RIP). RIP is a major component of the death receptor complex and has been shown to interact with Fas and tumor necrosis factor receptor 1 through its binding to adapter proteins. We have shown that RIP provides proapoptotic signals that are suppressed by its binding to FAK. We thus propose that FAK overexpression in human tumors provides a survival signal function by binding to RIP and inhibiting its interaction with the death receptor complex.
引用
收藏
页码:4361 / 4371
页数:11
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