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http://purl.uniprot.org/citations/10849009http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10849009http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10849009http://www.w3.org/2000/01/rdf-schema#comment"Phorbol esters reactivate Epstein-Barr virus (EBV) from latently infected cells via transcriptional activation of the viral immediate-early gene BZLF1. BZLF1 is a member of the extended AP-1 family of transcription factors that binds to specific BZLF1-binding motifs within early EBV promoters and to consensus AP-1 sites. Regulation of BZLF1's activity is achieved at the transcriptional level as well as through post-translational modifications. Recently, we reported that the transcriptional activity of BZLF1 is augmented by TPA [Baumann, M., Mischak, H., Dammeier, S., Kolch, W., Gires, O., Pich, D., Zeidler, R., Delecluse, H. J. & Hammerschmidt, W., (1998) J. Virol. 72, 8105-8114]. The increase of BZLF1's activity depends on a single serine residue (S186) that is phosphorylated by protein kinase C (PKC) in vitro and in vivo after stimulation with 12-O-tetradecanoylphorbol-13-acetate (TPA). Here, we identified RACK1 as a binding partner of BZLF1 in a yeast interaction trap assay. RACK stands for receptor of activated C-kinase and is involved in targeting activated PKCs and other signaling proteins. In vivo, RACK1 binds directly to the transactivation domain of BZLF1. Although a functional relationship between BZLF1 and PKC could be mediated by RACKs, RACK1 did not have a detectable effect on the phosphorylation status of BZLF1 in in vitro or in vivo phosphorylation assays. We suggest that RACK1 may act as a scaffolding protein on BZLF1 independently of activated PKCs."xsd:string
http://purl.uniprot.org/citations/10849009http://purl.org/dc/terms/identifier"doi:10.1046/j.1432-1327.2000.01430.x"xsd:string
http://purl.uniprot.org/citations/10849009http://purl.org/dc/terms/identifier"doi:10.1046/j.1432-1327.2000.01430.x"xsd:string
http://purl.uniprot.org/citations/10849009http://purl.uniprot.org/core/author"Baumann M."xsd:string
http://purl.uniprot.org/citations/10849009http://purl.uniprot.org/core/author"Baumann M."xsd:string
http://purl.uniprot.org/citations/10849009http://purl.uniprot.org/core/author"Gires O."xsd:string
http://purl.uniprot.org/citations/10849009http://purl.uniprot.org/core/author"Gires O."xsd:string
http://purl.uniprot.org/citations/10849009http://purl.uniprot.org/core/author"Hammerschmidt W."xsd:string
http://purl.uniprot.org/citations/10849009http://purl.uniprot.org/core/author"Hammerschmidt W."xsd:string
http://purl.uniprot.org/citations/10849009http://purl.uniprot.org/core/author"Kolch W."xsd:string
http://purl.uniprot.org/citations/10849009http://purl.uniprot.org/core/author"Kolch W."xsd:string
http://purl.uniprot.org/citations/10849009http://purl.uniprot.org/core/author"Mischak H."xsd:string
http://purl.uniprot.org/citations/10849009http://purl.uniprot.org/core/author"Mischak H."xsd:string
http://purl.uniprot.org/citations/10849009http://purl.uniprot.org/core/author"Pich D."xsd:string
http://purl.uniprot.org/citations/10849009http://purl.uniprot.org/core/author"Pich D."xsd:string
http://purl.uniprot.org/citations/10849009http://purl.uniprot.org/core/author"Zeidler R."xsd:string
http://purl.uniprot.org/citations/10849009http://purl.uniprot.org/core/author"Zeidler R."xsd:string
http://purl.uniprot.org/citations/10849009http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/10849009http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/10849009http://purl.uniprot.org/core/name"Eur. J. Biochem."xsd:string
http://purl.uniprot.org/citations/10849009http://purl.uniprot.org/core/name"Eur. J. Biochem."xsd:string
http://purl.uniprot.org/citations/10849009http://purl.uniprot.org/core/pages"3891-3901"xsd:string
http://purl.uniprot.org/citations/10849009http://purl.uniprot.org/core/pages"3891-3901"xsd:string