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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 , cytosol , mitochondrion , c jun , chemistry , dna fragmentation , caspase , p38 mitogen activated protein kinases , bcl 2 associated x protein , cytochrome , caspase 3 , 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.