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http://purl.uniprot.org/citations/9360956http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9360956http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9360956http://www.w3.org/2000/01/rdf-schema#comment"14-3-3 proteins mediate interactions between proteins involved in signal transduction and cell cycle regulation. Phosphorylation of target proteins as well as 14-3-3 are important for protein-protein interactions. Here, we describe the purification of a protein kinase from porcine brain that phosphorylates 14-3-3 zeta on Thr-233. This protein kinase has been identified as casein kinase Ialpha (CKIalpha) by peptide mapping analysis and sequencing. Among mammalian 14-3-3, only 14-3-3 tau possesses a phosphorylatable residue at the same position (Ser-233), and we show that this residue is also phosphorylated by CKI. In addition, we show that 14-3-3 zeta is exclusively phosphorylated on Thr-233 in human embryonic kidney 293 cells. The residue 233 is located within a region shown to be important for the association of 14-3-3 to target proteins. We showed previously that, in 293 cells, only the unphosphorylated form of 14-3-3 zeta associates with the regulatory domain of c-Raf. We have now shown that in vivo phosphorylation of 14-3-3 zeta at the CKIalpha site (Thr-233) negatively regulates its binding to c-Raf, and may be important in Raf-mediated signal transduction."xsd:string
http://purl.uniprot.org/citations/9360956http://purl.org/dc/terms/identifier"doi:10.1074/jbc.272.46.28882"xsd:string
http://purl.uniprot.org/citations/9360956http://purl.org/dc/terms/identifier"doi:10.1074/jbc.272.46.28882"xsd:string
http://purl.uniprot.org/citations/9360956http://purl.uniprot.org/core/author"Aitken A."xsd:string
http://purl.uniprot.org/citations/9360956http://purl.uniprot.org/core/author"Aitken A."xsd:string
http://purl.uniprot.org/citations/9360956http://purl.uniprot.org/core/author"Dubois T."xsd:string
http://purl.uniprot.org/citations/9360956http://purl.uniprot.org/core/author"Dubois T."xsd:string
http://purl.uniprot.org/citations/9360956http://purl.uniprot.org/core/author"Howell S."xsd:string
http://purl.uniprot.org/citations/9360956http://purl.uniprot.org/core/author"Howell S."xsd:string
http://purl.uniprot.org/citations/9360956http://purl.uniprot.org/core/author"Morrice N."xsd:string
http://purl.uniprot.org/citations/9360956http://purl.uniprot.org/core/author"Morrice N."xsd:string
http://purl.uniprot.org/citations/9360956http://purl.uniprot.org/core/author"Moelling K."xsd:string
http://purl.uniprot.org/citations/9360956http://purl.uniprot.org/core/author"Moelling K."xsd:string
http://purl.uniprot.org/citations/9360956http://purl.uniprot.org/core/author"Rommel C."xsd:string
http://purl.uniprot.org/citations/9360956http://purl.uniprot.org/core/author"Rommel C."xsd:string
http://purl.uniprot.org/citations/9360956http://purl.uniprot.org/core/author"Soneji Y."xsd:string
http://purl.uniprot.org/citations/9360956http://purl.uniprot.org/core/author"Soneji Y."xsd:string
http://purl.uniprot.org/citations/9360956http://purl.uniprot.org/core/author"Steinhussen U."xsd:string
http://purl.uniprot.org/citations/9360956http://purl.uniprot.org/core/author"Steinhussen U."xsd:string
http://purl.uniprot.org/citations/9360956http://purl.uniprot.org/core/date"1997"xsd:gYear
http://purl.uniprot.org/citations/9360956http://purl.uniprot.org/core/date"1997"xsd:gYear
http://purl.uniprot.org/citations/9360956http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/9360956http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string