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dc.contributor.authorTzivion, Guri
dc.contributor.authorLuo, Zhi-Jun
dc.contributor.authorAvruch, Joseph
dc.date.accessioned2019-10-05T03:27:55Z
dc.date.issued2000
dc.identifier.citationTzivion, Guri, Zhi-Jun Luo, and Joseph Avruch. 2000. “Calyculin A-Induced Vimentin Phosphorylation Sequesters 14-3-3 and Displaces Other 14-3-3 Partnersin Vivo.” Journal of Biological Chemistry 275 (38): 29772–78. https://doi.org/10.1074/jbc.m001207200.
dc.identifier.issn0021-9258
dc.identifier.issn1083-351X
dc.identifier.urihttp://nrs.harvard.edu/urn-3:HUL.InstRepos:41482968*
dc.description.abstract14-3-3 proteins bind their targets through a specific serine/threonine-phosphorylated motif present on the target protein. This binding is a crucial step in the phosphorylation-dependent regulation of various key proteins involved in signal transduction and cell cycle control, We report that treatment of COS-7 cells with the phosphatase inhibitor calyculin A induces association of 14-3-3 with a 55-kDa protein, identified as the intermediate filament protein vimentin, Association of vimentin with 14-3-3 depends on vimentin phosphorylation and requires the phosphopeptide-binding domain of 14-3-3, The region necessary for binding to 14-3-3 is confined to the vimentin amino-terminal head domain (amino acids 1-96). Monomeric forms of 14-3-3 do not bind vimentin in vivo or in vitro, indicating that a stable complex requires the binding of a 14-3-3 dimer to two sites on a single vimentin polypeptide. The calyculin A-induced association of vimentin with 14-3-3 in vivo results in the displacement of most other 14-3-3 partners, including the protooncogene Raf, which nevertheless remain capable of binding 14-3-3 in vitro, Concomitant with 14-3-3 displacement, calyculin A treatment blocks Raf activation by EGF; however, this inhibition is completely overcome by 14-3-3 overexpression in vivo or by the addition of prokaryotic recombinant 14-3-3 in vitro, Thus, phosphovimentin, by sequestering 14-3-3 and limiting its availability to other target proteins can affect intracellular signaling processes that require 14-3-3.
dc.language.isoen_US
dc.publisherAmerican Society for Biochemistry and Molecular Biology
dash.licenseLAA
dc.titleCalyculin A-induced Vimentin Phosphorylation Sequesters 14-3-3 and Displaces Other 14-3-3 Partners in Vivo
dc.typeJournal Article
dc.description.versionVersion of Record
dc.relation.journalThe Journal of Biological Chemistry
dash.depositing.authorAvruch, Joseph::9aac9685759478ee19677d9b77258031::600
dc.date.available2019-10-05T03:27:55Z
dash.workflow.comments1Science Serial ID 105751
dc.identifier.doi10.1074/jbc.M001207200
dash.source.volume275;38
dash.source.page29772-29778


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