Selective activation of JNK1 is necessary for the anti-apoptotic activity of hILP.
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.
Sanna
M G
MG
The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
Duckett
C S
CS
Richter
B W
BW
Thompson
C B
CB
Ulevitch
R J
RJ
D000818:Animals; D017209:Apoptosis / Q000187:drug effects / Q000502:physiology*; D019556:COS Cells; D017871:Calcium-Calmodulin-Dependent Protein Kinases / Q000502:physiology*; D003546:Cysteine Endopeptidases / Q000494:pharmacology; D004789:Enzyme Activation; D006801:Humans; D048031:JNK Mitogen-Activated Protein Kinases; D020928:Mitogen-Activated Protein Kinases; D011506:Proteins / Q000502:physiology*; D015398:Signal Transduction / Q000502:physiology*; D014162:Transfection; D051636:X-Linked Inhibitor of Apoptosis Protein
D011506:Proteins; D051636:X-Linked Inhibitor of Apoptosis Protein; C496866:XIAP protein, human; D017871:Calcium-Calmodulin-Dependent Protein Kinases; D048031:JNK Mitogen-Activated Protein Kinases; D020928:Mitogen-Activated Protein Kinases; D003546:Cysteine Endopeptidases