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

Proc Natl Acad Sci U S A. 1998 May 26;95(11):6015-20. doi: 10.1073/pnas.95.11.6015.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Apoptosis / drug effects
  • Apoptosis / physiology*
  • COS Cells
  • Calcium-Calmodulin-Dependent Protein Kinases / physiology*
  • Cysteine Endopeptidases / pharmacology
  • Enzyme Activation
  • Humans
  • JNK Mitogen-Activated Protein Kinases
  • Mitogen-Activated Protein Kinases*
  • Proteins / physiology*
  • Signal Transduction / physiology*
  • Transfection
  • X-Linked Inhibitor of Apoptosis Protein

Substances

  • Proteins
  • X-Linked Inhibitor of Apoptosis Protein
  • XIAP protein, human
  • Calcium-Calmodulin-Dependent Protein Kinases
  • JNK Mitogen-Activated Protein Kinases
  • Mitogen-Activated Protein Kinases
  • Cysteine Endopeptidases