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JNK phosphorylation of Bim-related members of the Bcl2 family induces Bax-dependent apoptosis.

The c-Jun NH(2)-terminal kinase (JNK) is activated when cells are exposed to environmental stress, including UV radiation. Gene disruption studies demonstrate that JNK is essential for UV-stimulated apoptosis mediated by the mitochondrial pathway by a Bax/Bak-dependent mechanism. Here, we demonstrate that JNK phosphorylates two members of the BH3-only subgroup of Bcl2-related proteins (Bim and Bmf) that are normally sequestered by binding to dynein and myosin V motor complexes. Phosphorylation by JNK causes release from the motor complexes. These proapoptotic BH3-only proteins therefore provide a molecular link between the JNK signal transduction pathway and the Bax/Bak-dependent mitochondrial apoptotic machinery.

Pubmed ID: 12591950


  • Lei K
  • Davis RJ


Proceedings of the National Academy of Sciences of the United States of America

Publication Data

March 4, 2003

Associated Grants


Mesh Terms

  • Adaptor Proteins, Signal Transducing
  • Apoptosis
  • Apoptosis Regulatory Proteins
  • Carrier Proteins
  • Cell Line
  • DNA Mutational Analysis
  • DNA, Complementary
  • Fibroblasts
  • Humans
  • Membrane Proteins
  • Mitochondria
  • Models, Biological
  • Neurons
  • Phosphorylation
  • Plasmids
  • Protein Binding
  • Protein Isoforms
  • Proto-Oncogene Proteins
  • Proto-Oncogene Proteins c-bcl-2
  • Signal Transduction
  • Threonine
  • bcl-2-Associated X Protein