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http://purl.uniprot.org/citations/19818711http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19818711http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19818711http://www.w3.org/2000/01/rdf-schema#comment"The Ski-interacting protein SKIP/SNW1 associates with the P-TEFb/CDK9 elongation factor and coactivates inducible genes, including HIV-1. We show here that SKIP also associates with c-Myc and Menin, a subunit of the MLL1 histone methyltransferase (H3K4me3) complex and that HIV-1 Tat transactivation requires c-Myc and Menin, but not MLL1 or H3K4me3. RNAi-ChIP experiments reveal that SKIP acts downstream of Tat:P-TEFb to recruit c-Myc and its partner TRRAP, a scaffold for histone acetyltransferases, to the HIV-1 promoter. By contrast, SKIP is recruited by the RNF20 H2B ubiquitin ligase to the basal HIV-1 promoter in a step that is bypassed by Tat and downregulated by c-Myc. Of interest, we find that SKIP and P-TEFb are dispensable for UV stress-induced HIV-1 transcription, which is strongly upregulated by treating cells with the CDK9 inhibitor flavopiridol. Thus, SKIP acts with c-Myc and Menin to promote HIV-1 Tat:P-TEFb transcription at an elongation step that is bypassed under stress."xsd:string
http://purl.uniprot.org/citations/19818711http://purl.org/dc/terms/identifier"doi:10.1016/j.molcel.2009.08.015"xsd:string
http://purl.uniprot.org/citations/19818711http://purl.org/dc/terms/identifier"doi:10.1016/j.molcel.2009.08.015"xsd:string
http://purl.uniprot.org/citations/19818711http://purl.uniprot.org/core/author"Yoshida T."xsd:string
http://purl.uniprot.org/citations/19818711http://purl.uniprot.org/core/author"Yoshida T."xsd:string
http://purl.uniprot.org/citations/19818711http://purl.uniprot.org/core/author"Jones K.A."xsd:string
http://purl.uniprot.org/citations/19818711http://purl.uniprot.org/core/author"Jones K.A."xsd:string
http://purl.uniprot.org/citations/19818711http://purl.uniprot.org/core/author"Bres V."xsd:string
http://purl.uniprot.org/citations/19818711http://purl.uniprot.org/core/author"Bres V."xsd:string
http://purl.uniprot.org/citations/19818711http://purl.uniprot.org/core/author"Pickle L."xsd:string
http://purl.uniprot.org/citations/19818711http://purl.uniprot.org/core/author"Pickle L."xsd:string
http://purl.uniprot.org/citations/19818711http://purl.uniprot.org/core/date"2009"xsd:gYear
http://purl.uniprot.org/citations/19818711http://purl.uniprot.org/core/date"2009"xsd:gYear
http://purl.uniprot.org/citations/19818711http://purl.uniprot.org/core/name"Mol. Cell"xsd:string
http://purl.uniprot.org/citations/19818711http://purl.uniprot.org/core/name"Mol. Cell"xsd:string
http://purl.uniprot.org/citations/19818711http://purl.uniprot.org/core/pages"75-87"xsd:string
http://purl.uniprot.org/citations/19818711http://purl.uniprot.org/core/pages"75-87"xsd:string
http://purl.uniprot.org/citations/19818711http://purl.uniprot.org/core/title"SKIP interacts with c-Myc and Menin to promote HIV-1 Tat transactivation."xsd:string
http://purl.uniprot.org/citations/19818711http://purl.uniprot.org/core/title"SKIP interacts with c-Myc and Menin to promote HIV-1 Tat transactivation."xsd:string
http://purl.uniprot.org/citations/19818711http://purl.uniprot.org/core/volume"36"xsd:string
http://purl.uniprot.org/citations/19818711http://purl.uniprot.org/core/volume"36"xsd:string
http://purl.uniprot.org/citations/19818711http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/19818711
http://purl.uniprot.org/citations/19818711http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/19818711