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dc.contributor.authorEnslen, Herve
dc.contributor.authorBrancho, Deborah Marie
dc.contributor.authorDavis, Roger J.
dc.date2022-08-11T08:08:57.000
dc.date.accessioned2022-08-23T16:13:40Z
dc.date.available2022-08-23T16:13:40Z
dc.date.issued2000-03-16
dc.date.submitted2008-09-04
dc.identifier.citationEMBO J. 2000 Mar 15;19(6):1301-11. <a href="http://dx.doi.org/10.1093/emboj/19.6.1301">Link to article on publisher's site</a>
dc.identifier.issn0261-4189 (Print)
dc.identifier.doi10.1093/emboj/19.6.1301
dc.identifier.pmid10716930
dc.identifier.urihttp://hdl.handle.net/20.500.14038/33678
dc.description.abstractThe p38 mitogen-activated protein kinase (MAPK) group is represented by four isoforms in mammals (p38alpha, p38beta2, p38gamma and p38delta). These p38 MAPK isoforms appear to mediate distinct functions in vivo due, in part, to differences in substrate phosphorylation by individual p38 MAPKs and also to selective activation by MAPK kinases (MAPKKs). Here we report the identification of two factors that contribute to the specificity of p38 MAPK activation. One mechanism of specificity is the selective formation of functional complexes between MAPKK and different p38 MAPKs. The formation of these complexes requires the presence of a MAPK docking site in the N-terminus of the MAPKK. The second mechanism that confers signaling specificity is the selective recognition of the activation loop (T-loop) of p38 MAPK isoforms. Together, these processes provide a mechanism that enables the selective activation of p38 MAPK in response to activated MAPKK.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=10716930&dopt=Abstract">Link to article in PubMed</a>
dc.relation.urlhttp://dx.doi.org/10.1093/emboj/19.6.1301
dc.subjectAmino Acid Motifs; Amino Acid Sequence; Amino Acid Substitution; Animals; COS Cells; Calcium-Calmodulin-Dependent Protein; Kinases; Enzyme Activation; Isoenzymes; MAP Kinase Kinase 3; MAP Kinase Kinase 6; MAP Kinase Signaling System; Mitogen-Activated Protein Kinase Kinases; *Mitogen-Activated Protein Kinases; Molecular Sequence Data; Phosphorylation; Phosphothreonine; Phosphotyrosine; Protein Binding; Protein-Tyrosine Kinases; Recombinant Fusion Proteins; Sequence Alignment; Sequence Deletion; Substrate Specificity; Transfection; p38 Mitogen-Activated Protein Kinases
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleMolecular determinants that mediate selective activation of p38 MAP kinase isoforms
dc.typeJournal Article
dc.source.journaltitleThe EMBO journal
dc.source.volume19
dc.source.issue6
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/gsbs_sp/343
dc.identifier.contextkey619055
html.description.abstract<p>The p38 mitogen-activated protein kinase (MAPK) group is represented by four isoforms in mammals (p38alpha, p38beta2, p38gamma and p38delta). These p38 MAPK isoforms appear to mediate distinct functions in vivo due, in part, to differences in substrate phosphorylation by individual p38 MAPKs and also to selective activation by MAPK kinases (MAPKKs). Here we report the identification of two factors that contribute to the specificity of p38 MAPK activation. One mechanism of specificity is the selective formation of functional complexes between MAPKK and different p38 MAPKs. The formation of these complexes requires the presence of a MAPK docking site in the N-terminus of the MAPKK. The second mechanism that confers signaling specificity is the selective recognition of the activation loop (T-loop) of p38 MAPK isoforms. Together, these processes provide a mechanism that enables the selective activation of p38 MAPK in response to activated MAPKK.</p>
dc.identifier.submissionpathgsbs_sp/343
dc.contributor.departmentHoward Hughes Medical Institute, Program in Molecular Medicine
dc.contributor.departmentGraduate School of Biomedical Sciences
dc.source.pages1301-11


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