Linked Life Data

17670986

Source:http://linkedlifedata.com/resource/pubmed/id/17670986

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pubmed-article:17670986pubmed:abstractTextAlthough oligodendrocytes undergo apoptosis after spinal cord injury, molecular mechanisms responsible for their death have been unknown. We report that oligodendrocyte apoptosis is regulated oppositely by c-Jun N-terminal kinase 3 (JNK3) and protein interacting with the mitotic kinase, never in mitosis A I (Pin1), the actions of which converge on myeloid cell leukemia sequence-1 (Mcl-1). Activated after injury, JNK3 induces cytochrome c release by facilitating the degradation of Mcl-1, the stability of which is maintained in part by Pin1. Pin1 binds Mcl-1 at its constitutively phosphorylated site, Thr163Pro, and stabilizes it by inhibiting ubiquitination. After injury JNK3 phosphorylates Mcl-1 at Ser121Pro, facilitating the dissociation of Pin1 from Mcl-1. JNK3 thus induces Mcl-1 degradation by counteracting the protective binding of Pin1. These results are confirmed by the opposing phenotypes observed between JNK3-/- and Pin1-/- mice: oligodendrocyte apoptosis and cytochrome c release are reduced in JNK3-/- but elevated in Pin1-/- mice. This report thus unveils a mechanism by which cytochrome c release is under the opposite control of JNK3 and Pin1, regulators for which the activities are intricately coupled.lld:pubmed
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pubmed-article:17670986pubmed:dateRevised2011-9-22lld:pubmed
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pubmed-article:17670986pubmed:articleTitleOpposite regulation of oligodendrocyte apoptosis by JNK3 and Pin1 after spinal cord injury.lld:pubmed
pubmed-article:17670986pubmed:affiliationCenter for Molecular Neurobiology and Department of Molecular and Cellular Biochemistry, The Ohio State University, Columbus, Ohio 43210, USA.lld:pubmed
pubmed-article:17670986pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:17670986pubmed:publicationTypeComparative Studylld:pubmed
pubmed-article:17670986pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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