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dc.contributor.authorChow, Chi-Wing
dc.contributor.authorRincon, Mercedes
dc.contributor.authorCavanagh, Julie
dc.contributor.authorDickens, Martin
dc.contributor.authorDavis, Roger J.
dc.date2022-08-11T08:09:35.000
dc.date.accessioned2022-08-23T16:36:30Z
dc.date.available2022-08-23T16:36:30Z
dc.date.issued1997-12-31
dc.date.submitted2009-03-31
dc.identifier.citation<p>Science. 1997 Nov 28;278(5343):1638-41.</p>
dc.identifier.issn0036-8075 (Print)
dc.identifier.doi10.1126/science.278.5343.1638
dc.identifier.pmid9374467
dc.identifier.urihttp://hdl.handle.net/20.500.14038/38801
dc.description.abstractThe nuclear factor of activated T cells (NFAT) group of transcription factors is retained in the cytoplasm of quiescent cells. NFAT activation is mediated in part by induced nuclear import. This process requires calcium-dependent dephosphorylation of NFAT caused by the phosphatase calcineurin. The c-Jun amino-terminal kinase (JNK) phosphorylates NFAT4 on two sites. Mutational removal of the JNK phosphorylation sites caused constitutive nuclear localization of NFAT4. In contrast, JNK activation in calcineurin-stimulated cells caused nuclear exclusion of NFAT4. These findings show that the nuclear accumulation of NFAT4 promoted by calcineurin is opposed by the JNK signal transduction pathway.
dc.language.isoen_US
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=9374467&dopt=Abstract">Link to Article in PubMed</a></p>
dc.relation.urlhttps://doi.org/10.1126/science.278.5343.1638
dc.subjectAnimals
dc.subjectBinding Sites
dc.subjectCOS Cells
dc.subjectCalcineurin
dc.subjectCalcium-Calmodulin-Dependent Protein Kinases
dc.subjectCell Line
dc.subjectCell Nucleus
dc.subjectCyclosporine
dc.subjectCytoplasm
dc.subjectDNA-Binding Proteins
dc.subjectHumans
dc.subjectJNK Mitogen-Activated Protein Kinases
dc.subjectJurkat Cells
dc.subjectMitogen-Activated Protein Kinase Kinases
dc.subject*Mitogen-Activated Protein Kinases
dc.subjectMutation
dc.subjectNFATC Transcription Factors
dc.subject*Nuclear Proteins
dc.subjectPhosphorylation
dc.subjectProtein Kinases
dc.subjectRecombinant Fusion Proteins
dc.subject*Signal Transduction
dc.subjectT-Lymphocytes
dc.subjectTranscription Factors
dc.subjectTranscription, Genetic
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleNuclear accumulation of NFAT4 opposed by the JNK signal transduction pathway
dc.typeJournal Article
dc.source.journaltitleScience (New York, N.Y.)
dc.source.volume278
dc.source.issue5343
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/oapubs/1645
dc.identifier.contextkey805466
html.description.abstract<p>The nuclear factor of activated T cells (NFAT) group of transcription factors is retained in the cytoplasm of quiescent cells. NFAT activation is mediated in part by induced nuclear import. This process requires calcium-dependent dephosphorylation of NFAT caused by the phosphatase calcineurin. The c-Jun amino-terminal kinase (JNK) phosphorylates NFAT4 on two sites. Mutational removal of the JNK phosphorylation sites caused constitutive nuclear localization of NFAT4. In contrast, JNK activation in calcineurin-stimulated cells caused nuclear exclusion of NFAT4. These findings show that the nuclear accumulation of NFAT4 promoted by calcineurin is opposed by the JNK signal transduction pathway.</p>
dc.identifier.submissionpathoapubs/1645
dc.contributor.departmentHoward Hughes Medical Institute and Program in Molecular Medicine
dc.source.pages1638-41


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