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

http://www.ncbi.nlm.nih.gov/pubmed/12591950

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 RIS Download

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

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Addgene (Reagent, Plasmid)

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