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dc.contributor.authorShen, Ying H.
dc.contributor.authorGodlewski, Jakub
dc.contributor.authorBronisz, Agnieszka
dc.contributor.authorZhu, Jun
dc.contributor.authorComb, Michael J.
dc.contributor.authorAvruch, Joseph
dc.contributor.authorTzivion, Guri
dc.date.accessioned2019-10-05T03:27:34Z
dc.date.issued2003
dc.identifier.citationShen, Ying H., Jakub Godlewski, Agnieszka Bronisz, Jun Zhu, Michael J. Comb, Joseph Avruch, and Guri Tzivion. 2003. “Significance of 14-3-3 Self-Dimerization for Phosphorylation-Dependent Target Binding.” Molecular Biology of the Cell 14 (11): 4721–33. https://doi.org/10.1091/mbc.e02-12-0821.
dc.identifier.issn1059-1524
dc.identifier.issn1939-4586
dc.identifier.urihttp://nrs.harvard.edu/urn-3:HUL.InstRepos:41482944*
dc.description.abstract14-3-3 proteins via binding serine/threonine-phosphorylated proteins regulate diverse intracellular processes in all eukaryotic organisms. Here, we examine the role of 14-3-3 self-dimerization in target binding, and in the susceptibility of 14-3-3 to undergo phosphorylation. Using a phospho-specific antibody developed against a degenerated mode-1 14-3-3 binding motif (RSxpSxP), we demonstrate that most of the 14-3-3-associated proteins in COS-7 cells are phosphorylated on sites that react with this antibody. The binding of these phosphoproteins depends on 14-3-3 dimerization, inasmuch as proteins associated in vivo with a monomeric 14-3-3 form are not recognized by the phospho-specific antibody. The role of 14-3-3 dimerization in the phosphorylation-dependent target binding is further exemplified with two well-defined 14-3-3 targets, Raf and DAF-16. Raf and DAF-16 can bind both monomeric and dimeric 14-3-3; however, whereas phosphorylation of specific Raf and DAF-16 sites is required for binding to dimeric 14-3-3, binding to monomeric 14-3-3 forms is entirely independent of Raf and DAF-16 phosphorylation. We also find that dimerization diminishes 14-3-3 susceptibility to phosphorylation. These findings establish a significant role of 14-3-3 dimerization in its ability to bind targets in a phosphorylation-dependent manner and point to a mechanism in which 14-3-3 phosphorylation and dimerization counterregulate each other.
dc.language.isoen_US
dc.publisherAmerican Society for Cell Biology
dash.licenseLAA
dc.titleSignificance of 14-3-3 Self-Dimerization for Phosphorylation-dependent Target Binding
dc.typeJournal Article
dc.description.versionVersion of Record
dc.relation.journalMolecular Biology of the Cell
dash.depositing.authorAvruch, Joseph::9aac9685759478ee19677d9b77258031::600
dc.date.available2019-10-05T03:27:34Z
dash.workflow.comments1Science Serial ID 64598
dc.identifier.doi10.1091/mbc.E02-12-0821
dash.source.volume14;11
dash.source.page4721


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