Open AccessSelective activation of JNK1 is necessary for the anti-apoptotic activity of hILP
Author(s) -
Marta Sanna,
Colin S. Duckett,
Bettina Richter,
Craig B. Thompson,
Richard J. Ulevitch
Publication year - 1998
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.95.11.6015
Subject(s) - apoptosis , microbiology and biotechnology , endogeny , biology , inhibitor of apoptosis domain , protein kinase a , programmed cell death , kinase , caspase , enzyme activator , enzyme , signal transduction , biochemistry
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.