UMMS Affiliation

Howard Hughes Medical Institute and Program in Molecular Medicine

Publication Date


Document Type



Animals; Apoptosis; Caspase 3; Caspases; Cells, Cultured; Cricetinae; Cytochrome c Group; Enzyme Activation; JNK Mitogen-Activated Protein Kinases; MAP Kinase Kinase 7; Membrane Proteins; Mice; Mitochondria; Mitogen-Activated Protein Kinase Kinases; Mitogen-Activated Protein Kinases; Phosphorylation; Proto-Oncogene Proteins; Proto-Oncogene Proteins c-bcl-2; Recombinant Proteins; *Signal Transduction; Transcription Factor AP-1; Ultraviolet Rays; bcl-2 Homologous Antagonist-Killer Protein; bcl-2-Associated X Protein


Life Sciences | Medicine and Health Sciences


Targeted gene disruption studies have established that the c-Jun NH(2)-terminal kinase (JNK) signaling pathway is required for stress-induced release of mitochondrial cytochrome c and apoptosis. Here we demonstrate that activated JNK is sufficient to induce rapid cytochrome c release and apoptosis. However, activated JNK fails to cause death in cells deficient of members of the Bax subfamily of proapoptotic Bcl2-related proteins. Furthermore, exposure to stress fails to activate Bax, cause cytochrome c release, and induce death in JNK-deficient cells. These data demonstrate that proapoptotic members of the Bax protein subfamily are essential for JNK-dependent apoptosis.


Mol Cell Biol. 2002 Jul;22(13):4929-42.

Journal/Book/Conference Title

Molecular and cellular biology

Related Resources

Link to Article in PubMed

PubMed ID