Please use this identifier to cite or link to this item: https://hdl.handle.net/2440/9538
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dc.contributor.authorWoodcock, J.-
dc.contributor.authorMurphy, J.-
dc.contributor.authorStomski, F.-
dc.contributor.authorBerndt, M.-
dc.contributor.authorLopez, A.-
dc.date.issued2003-
dc.identifier.citationJournal of Biological Chemistry, 2003; 278(38):36323-36327-
dc.identifier.issn0021-9258-
dc.identifier.issn1083-351X-
dc.identifier.urihttp://hdl.handle.net/2440/9538-
dc.description.abstractThe 14-3-3 proteins play a central role in the regulation of cell growth, cycling, and apoptosis by modulating the functional activities of key signaling proteins. Through binding to a phosphoserine motif, 14-3-3 alters target proteins activities by sequestering them, relocalizing them, conformationally altering their functional activity, or by promoting interaction with other proteins. These functions of 14-3-3 are facilitated by, if not dependent on, its dimeric structure. We now show that the dimeric status of 14-3-3 is regulated by site-specific serine phosphorylation. We found that a sphingosine-dependent kinase phosphorylates 14-3-3 in vitro and in vivo on a serine residue (Ser58) located within the dimer interface. Furthermore, by developing an antibody that specifically recognizes 14-3-3zeta phosphorylated on Ser58 and employing native-PAGE and cross-linking techniques, we found that 14-3-3 phosphorylated on Ser58 is monomeric both in vitro and in vivo. Phosphorylated 14-3-3 was detected solely as a monomer, indicating that phosphorylation of a single monomer within a dimer is sufficient to disrupt the dimeric structure. Significantly, phosphorylation-induced monomerization did not prevent 14-3-3 binding to a phosphopeptide target. We propose that this regulated monomerization of 14-3-3 controls its ability to modulate the activity of target proteins and thus may have significant implications for 14-3-3 function and the regulation of many cellular processes.-
dc.description.statementofresponsibilityJoanna M. Woodcock, Jane Murphy, Frank C. Stomski, Michael C. Berndt, and Angel F. Lopez-
dc.language.isoen-
dc.publisherAmer Soc Biochemistry Molecular Biology Inc-
dc.source.urihttp://dx.doi.org/10.1074/jbc.m304689200-
dc.subjectNIH 3T3 Cells-
dc.subjectAnimals-
dc.subjectMice, Inbred BALB C-
dc.subjectRabbits-
dc.subjectMice-
dc.subjectTyrosine 3-Monooxygenase-
dc.subjectSerine-
dc.subject14-3-3 Proteins-
dc.subjectRecombinant Proteins-
dc.subjectCross-Linking Reagents-
dc.subjectImmunoblotting-
dc.subjectElectrophoresis, Polyacrylamide Gel-
dc.subjectSignal Transduction-
dc.subjectApoptosis-
dc.subjectAmino Acid Motifs-
dc.subjectProtein Conformation-
dc.subjectProtein Binding-
dc.subjectDimerization-
dc.subjectPhosphorylation-
dc.titleThe dimeric versus monomeric status of 14-3-3z is controlled by phosphorylation of Ser58 at the dimer interface-
dc.typeJournal article-
dc.identifier.doi10.1074/jbc.M304689200-
pubs.publication-statusPublished-
dc.identifier.orcidLopez, A. [0000-0001-7430-0135]-
Appears in Collections:Aurora harvest
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