西亞試劑：Inactivation of BAD by IKK Inhibits TNFα-Induced Apoptosis

Inactivation of BAD by IKK Inhibits TNFα-Induced Apoptosis Independently of NF-B Activation

Jie Yan, Jialing Xiang, Yutin Lin, Jingui Ma, Jiyan Zhang,Hao Zhang, Jisheng Sun, Nika N. Danial, Jing Liu and Anning Lin

The IB kinase complex (IKK) is a key regulator of immune responses, inflammation, cell survival, and tumorigenesis. The prosurvival function of IKK centers on activation of the transcription factor NF-B, whose target gene products inhibit caspases and prevent prolonged JNK activation. Here, we report that inactivation of the BH3-only protein BAD by IKK independently of NF-B activation suppresses TNFα-induced apoptosis. TNFα-treated Ikkβ/ mouse embryonic fibroblasts (MEFs) undergo apoptosis significantly faster than MEFs deficient in both RelA and cRel due to lack of inhibition of BAD by IKK. IKK phosphorylates BAD at serine-26 (Ser26) and primes it for inactivation. Elimination of Ser26 phosphorylation promotes BAD proapoptotic activity, thereby accelerating TNFα-induced apoptosis in cultured cells and increasing mortality in animals. Our results reveal that IKK inhibits TNFα-induced apoptosis through two distinct but cooperative mechanisms: activation of the survival factor NF-B and inactivation of the proapoptotic BH3-only BAD protein.

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