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




To view the content in your browser, please download Adobe Reader or, alternately,
you may Download the file to your hard drive.

NOTE: The latest versions of Adobe Reader do not support viewing PDF files within Firefox on Mac OS and if you are using a modern (Intel) Mac, there is no official plugin for viewing PDF files within the browser window.