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JNK interaction with Sab mediates ER stress induced inhibition of mitochondrial respiration and cell death

AuthorsWin, Sanda; Than, Tinaung; Fernández-Checa, José C. ; Kaplowitz, Neil
HeLa cells
Signal transduction
Oxidative stress
Reactive oxygen species
Issue Date9-Jan-2014
PublisherNature Publishing Group
CitationCell Death & Disease 5(1): e989 (2014)
AbstractOur aim was to better understand the mechanism and importance of sustained c-Jun N-terminal kinase (JNK) activation in endoplasmic reticulum (ER) stress and effects of ER stress on mitochondria by determining the role of mitochondrial JNK binding protein, Sab. Tunicamycin or brefeldin A induced a rapid and marked decline in basal mitochondrial respiration and reserve-capacity followed by delayed mitochondrial-mediated apoptosis. Knockdown of mitochondrial Sab prevented ER stress-induced sustained JNK activation, impaired respiration, and apoptosis, but did not alter the magnitude or time course of activation of ER stress pathways. P-JNK plus adenosine 5'-triphosphate (ATP) added to isolated liver mitochondria promoted superoxide production, which was amplified by addition of calcium and inhibited by a blocking peptide corresponding to the JNK binding site on Sab (KIM1). This peptide also blocked tunicamycin-induced inhibition of cellular respiration. In conclusion, ER stress triggers an interaction of JNK with mitochondrial Sab, which leads to impaired respiration and increased mitochondrial reactive oxygen species, sustaining JNK activation culminating in apoptosis.
Publisher version (URL)http://dx.doi.org/10.1038/cddis.2013.522
Identifiersdoi: 10.1038/cddis.2013.522
issn: 2041-4889
Appears in Collections:(IIBB) Artículos
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