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Proc Natl Acad Sci U S A. 1998 May 26;95(11):6015-20.

Selective activation of JNK1 is necessary for the anti-apoptotic activity of hILP.

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  • 1The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.


The balance between the inductive signals and endogenous anti-apoptotic mechanisms determines whether or not programmed cell death occurs. The widely expressed inhibitor of apoptosis gene family includes three closely related mammalian proteins: c-IAP1, c-IAP2, and hILP. The anti-apoptotic properties of these proteins have been linked to caspase inhibition. Here we show that one member of this group, hILP, inhibits interleukin-1beta-converting enzyme-induced apoptosis via a mechanism dependent on the selective activation of c-Jun N-terminal kinase 1. These data demonstrate that apoptosis can be inhibited by an endogenous cellular protein by a mechanism that requires the activation of a single member of the mitogen-activating protein kinase family.

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