Selective activation of JNK1 is necessary for the anti-apoptotic activity of hILP
MG Sanna, CS Duckett, BWM Richter… - Proceedings of the …, 1998 - National Acad Sciences
MG Sanna, CS Duckett, BWM Richter, CB Thompson, RJ Ulevitch
Proceedings of the National Academy of Sciences, 1998•National Acad SciencesThe 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-1β-
converting enzyme-induced apoptosis via a mechanism dependent on the selective …
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-1β-
converting enzyme-induced apoptosis via a mechanism dependent on the selective …
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-1β-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.
National Acad Sciences