The regulation of Bax by c‐Jun N‐terminal protein kinase (JNK) is a prerequisite to the mitochondrial‐induced apoptotic pathway | Zendy

Papadakis Emmanouil S. | Zendy; Finegan Katherine G. | Zendy; Wang Xin | Zendy; Robinson Andrew C. | Zendy; Guo Chun | Zendy; Kayahara Midori | Zendy; Tournier Cathy | Zendy

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The regulation of Bax by c‐Jun N‐terminal protein kinase (JNK) is a prerequisite to the mitochondrial‐induced apoptotic pathway

Author(s) -

Papadakis Emmanouil S.,

Finegan Katherine G.,

Wang Xin,

Robinson Andrew C.,

Guo Chun,

Kayahara Midori,

Tournier Cathy

Publication year - 2006

Publication title -

febs letters

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.593

H-Index - 257

eISSN - 1873-3468

pISSN - 0014-5793

DOI - 10.1016/j.febslet.2006.01.053

Subject(s) - cytochrome c , apoptosis , microbiology and biotechnology , kinase , mitochondrion , cytosol , dna fragmentation , c jun , chemistry , caspase , bcl 2 associated x protein , p38 mitogen activated protein kinases , caspase 3 , cytochrome , programmed cell death , protein kinase a , biology , biochemistry , transcription factor , gene , enzyme

The signaling mechanism by which JNK affects mitochondria is critical to initiate apoptosis. Here we show that the absence of JNK provides a partial resistance to the toxic effect of the heavy metal cadmium. Both wild type and jnk −/− fibroblasts undergoing death exhibit cytosolic cytochrome c but, unlike wild type cells, the JNK‐deficient fibroblasts do not display increased caspase activity and DNA fragmentation. The absence of apoptotic death correlates with a specific defect in activation of Bax. We conclude that JNK‐dependent regulation of Bax is essential to mediate the apoptotic release of cytochrome c regardless of Bid and Bim activation.

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