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dc.contributor.authorMorel, Caroline
dc.contributor.authorCarlson, Scott M.
dc.contributor.authorWhite, Forest M.
dc.contributor.authorDavis, Roger J.
dc.date2022-08-11T08:09:39.000
dc.date.accessioned2022-08-23T16:39:02Z
dc.date.available2022-08-23T16:39:02Z
dc.date.issued2009-05-13
dc.date.submitted2010-04-06
dc.identifier.citationMol Cell Biol. 2009 Jul;29(14):3845-52. Epub 2009 May 11. <a href="http://dx.doi.org/10.1128/MCB.00279-09">Link to article on publisher's site</a>
dc.identifier.issn0270-7306 (Linking)
dc.identifier.doi10.1128/MCB.00279-09
dc.identifier.pmid19433446
dc.identifier.urihttp://hdl.handle.net/20.500.14038/39382
dc.description.abstractMcl-1 is a member of the Bcl2-related protein family that is a critical mediator of cell survival. Exposure of cells to stress causes inhibition of Mcl-1 mRNA translation and rapid destruction of Mcl-1 protein by proteasomal degradation mediated by a phosphodegron created by glycogen synthase kinase 3 (GSK3) phosphorylation of Mcl-1. Here we demonstrate that prior phosphorylation of Mcl-1 by the c-Jun N-terminal protein kinase (JNK) is essential for Mcl-1 phosphorylation by GSK3. Stress-induced Mcl-1 degradation therefore requires the coordinated activity of JNK and GSK3. Together, these data establish that Mcl-1 functions as a site of signal integration between the proapoptotic activity of JNK and the prosurvival activity of the AKT pathway that inhibits GSK3.
dc.language.isoen_US
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=19433446&dopt=Abstract">Link to Article in PubMed</a></p>
dc.relation.urlhttp://dx.doi.org/10.1128/MCB.00279-09
dc.rightsPublisher PDF posted as allowed by the publisher's author rights policy at http://journals.asm.org/site/misc/ASM_Author_Statement.xhtml.
dc.subjectBiochemistry
dc.subjectCell Biology
dc.subjectCellular and Molecular Physiology
dc.subjectMolecular Biology
dc.titleMcl-1 integrates the opposing actions of signaling pathways that mediate survival and apoptosis
dc.typeJournal Article
dc.source.journaltitleMolecular and cellular biology
dc.source.volume29
dc.source.issue14
dc.identifier.legacyfulltexthttps://escholarship.umassmed.edu/cgi/viewcontent.cgi?article=3178&amp;context=oapubs&amp;unstamped=1
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/oapubs/2179
dc.identifier.contextkey1262959
refterms.dateFOA2022-08-23T16:39:02Z
html.description.abstract<p>Mcl-1 is a member of the Bcl2-related protein family that is a critical mediator of cell survival. Exposure of cells to stress causes inhibition of Mcl-1 mRNA translation and rapid destruction of Mcl-1 protein by proteasomal degradation mediated by a phosphodegron created by glycogen synthase kinase 3 (GSK3) phosphorylation of Mcl-1. Here we demonstrate that prior phosphorylation of Mcl-1 by the c-Jun N-terminal protein kinase (JNK) is essential for Mcl-1 phosphorylation by GSK3. Stress-induced Mcl-1 degradation therefore requires the coordinated activity of JNK and GSK3. Together, these data establish that Mcl-1 functions as a site of signal integration between the proapoptotic activity of JNK and the prosurvival activity of the AKT pathway that inhibits GSK3.</p>
dc.identifier.submissionpathoapubs/2179
dc.contributor.departmentProgram in Molecular Medicine
dc.source.pages3845-52


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