Phosphorylation and inactivation of myeloid cell leukemia 1 by JNK in response to oxidative stress.
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Inoshita S, Takeda K, Hatai T, Terada Y, Sano M, Hata J, Umezawa A, Ichijo H
Phosphorylation and inactivation of myeloid cell leukemia 1 by JNK in response to oxidative stress.
J Biol Chem. 2002 Nov 15;277(46):43730-4. Epub 2002 Sep 9.
- PubMed ID
- 12223490 [ View in PubMed]
- Abstract
Oxidative stress induces JNK activation, which leads to apoptosis through mitochondria-dependent caspase activation. However, little is known about the mechanism by which JNK alters mitochondrial function. In this study, we investigated the role of phosphorylation of myeloid cell leukemia 1 (Mcl-1), an anti-apoptotic member of the Bcl-2 family, in oxidative stress-induced apoptosis. We found that JNK phosphorylated Ser-121 and Thr-163 of Mcl-1 in response to stimulation with H(2)O(2) and that transfection of unphosphorylatable Mcl-1 resulted in an enhanced anti-apoptotic activity in response to stimulation with H(2)O(2). JNK-dependent phosphorylation and thus inactivation of Mcl-1 may be one of the mechanisms through which oxidative stress induces cellular damage.