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http://purl.uniprot.org/citations/21220424http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21220424http://www.w3.org/2000/01/rdf-schema#comment"Reversible acetylation of Tat is critical for its transactivation activity toward HIV-1 transcription. However, the enzymes involved in the acetylation/deacetylation cycles have not been fully characterized. In this study, by yeast two-hybrid assay, we have discovered the histone deacetylase HDAC6 to be a binding partner of Tat. Our data show that HDAC6 interacts with Tat in the cytoplasm in a microtubule-dependent manner. In addition, HDAC6 deacetylates Tat at Lys-28 and thereby suppresses Tat-mediated transactivation of the HIV-1 promoter. Inactivation of HDAC6 promotes the interaction of Tat with cyclin T1 and leads to an increase in Tat transactivation activity. These findings establish HDAC6 as a Tat deacetylase and support a model in which Lys-28 deacetylation decreases Tat transactivation activity through affecting the ability of Tat to form a ribonucleoprotein complex with cyclin T1 and the transactivation-responsive RNA."xsd:string
http://purl.uniprot.org/citations/21220424http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m110.208884"xsd:string
http://purl.uniprot.org/citations/21220424http://purl.uniprot.org/core/author"Liu M."xsd:string
http://purl.uniprot.org/citations/21220424http://purl.uniprot.org/core/author"Li D."xsd:string
http://purl.uniprot.org/citations/21220424http://purl.uniprot.org/core/author"Sun X."xsd:string
http://purl.uniprot.org/citations/21220424http://purl.uniprot.org/core/author"Shi X."xsd:string
http://purl.uniprot.org/citations/21220424http://purl.uniprot.org/core/author"Zhou J."xsd:string
http://purl.uniprot.org/citations/21220424http://purl.uniprot.org/core/author"Yang W."xsd:string
http://purl.uniprot.org/citations/21220424http://purl.uniprot.org/core/author"Qiao W."xsd:string
http://purl.uniprot.org/citations/21220424http://purl.uniprot.org/core/author"Huo L."xsd:string
http://purl.uniprot.org/citations/21220424http://purl.uniprot.org/core/author"Aneja R."xsd:string
http://purl.uniprot.org/citations/21220424http://purl.uniprot.org/core/author"Karna P."xsd:string
http://purl.uniprot.org/citations/21220424http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/21220424http://purl.uniprot.org/core/name"J Biol Chem"xsd:string
http://purl.uniprot.org/citations/21220424http://purl.uniprot.org/core/pages"9280-9286"xsd:string
http://purl.uniprot.org/citations/21220424http://purl.uniprot.org/core/title"Regulation of Tat acetylation and transactivation activity by the microtubule-associated deacetylase HDAC6."xsd:string
http://purl.uniprot.org/citations/21220424http://purl.uniprot.org/core/volume"286"xsd:string
http://purl.uniprot.org/citations/21220424http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/21220424
http://purl.uniprot.org/citations/21220424http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/21220424
http://purl.uniprot.org/uniprot/#_B3KT76-mappedCitation-21220424http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/21220424
http://purl.uniprot.org/uniprot/#_B3KVK5-mappedCitation-21220424http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/21220424
http://purl.uniprot.org/uniprot/#_B3KNA1-mappedCitation-21220424http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/21220424
http://purl.uniprot.org/uniprot/#_B3KMC3-mappedCitation-21220424http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/21220424
http://purl.uniprot.org/uniprot/#_B3KY98-mappedCitation-21220424http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/21220424