RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/12606581http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12606581http://www.w3.org/2000/01/rdf-schema#comment"Microtubules are cylindrical cytoskeletal structures found in almost all eukaryotic cell types which are involved in a great variety of cellular processes. Reversible acetylation on the epsilon-amino group of alpha-tubulin Lys40 marks stabilized microtubule structures and may contribute to regulating microtubule dynamics. Yet, the enzymes catalysing this acetylation/deacetylation have remained unidentified until recently. Here we report that beta-tubulin interacts with histone deacetylase-6 (HDAC-6) in a yeast two-hybrid assay and in vitro. We find that HDAC-6 is a micro tubule-associated protein capable of deacetylating alpha-tubulin in vivo and in vitro. HDAC-6's microtubule binding and deacetylation functions both depend on the hdac domains. Overexpression of HDAC-6 in mammalian cells leads to tubulin hypoacetylation. In contrast, inhibition of HDAC-6 function by two independent mechanisms--pharmacological (HDAC inhibitors) or genetic (targeted inactivation of HDAC-6 in embryonic stem cells)--leads to hyperacetylation of tubulin and microtubules. Taken together, our data provide evidence that HDAC-6 might act as a dual deacetylase for tubulin and histones, and suggest the possibility that acetylated non-histone proteins might represent novel targets for pharmacological therapy by HDAC inhibitors."xsd:string
http://purl.uniprot.org/citations/12606581http://purl.org/dc/terms/identifier"doi:10.1093/emboj/cdg115"xsd:string
http://purl.uniprot.org/citations/12606581http://purl.uniprot.org/core/author"Li N."xsd:string
http://purl.uniprot.org/citations/12606581http://purl.uniprot.org/core/author"Hess D."xsd:string
http://purl.uniprot.org/citations/12606581http://purl.uniprot.org/core/author"Zhang Y."xsd:string
http://purl.uniprot.org/citations/12606581http://purl.uniprot.org/core/author"Caron C."xsd:string
http://purl.uniprot.org/citations/12606581http://purl.uniprot.org/core/author"Khochbin S."xsd:string
http://purl.uniprot.org/citations/12606581http://purl.uniprot.org/core/author"Matthias P."xsd:string
http://purl.uniprot.org/citations/12606581http://purl.uniprot.org/core/author"Matthias G."xsd:string
http://purl.uniprot.org/citations/12606581http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12606581http://purl.uniprot.org/core/name"EMBO J"xsd:string
http://purl.uniprot.org/citations/12606581http://purl.uniprot.org/core/pages"1168-1179"xsd:string
http://purl.uniprot.org/citations/12606581http://purl.uniprot.org/core/title"HDAC-6 interacts with and deacetylates tubulin and microtubules in vivo."xsd:string
http://purl.uniprot.org/citations/12606581http://purl.uniprot.org/core/volume"22"xsd:string
http://purl.uniprot.org/citations/12606581http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12606581
http://purl.uniprot.org/citations/12606581http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/12606581
http://purl.uniprot.org/uniprot/Q9Z2V5#attribution-951013C716EFD27922C062B26B6F67C4http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/12606581
http://purl.uniprot.org/uniprot/#_A0A1B0GX25-mappedCitation-12606581http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/12606581
http://purl.uniprot.org/uniprot/#_B1AUA8-mappedCitation-12606581http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/12606581
http://purl.uniprot.org/uniprot/#_B1AUA9-mappedCitation-12606581http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/12606581
http://purl.uniprot.org/uniprot/#_Q3U4Q5-mappedCitation-12606581http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/12606581
http://purl.uniprot.org/uniprot/#_Q3UG37-mappedCitation-12606581http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/12606581
http://purl.uniprot.org/uniprot/#_Q8CGC3-mappedCitation-12606581http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/12606581
http://purl.uniprot.org/uniprot/#_Q9Z2V5-mappedCitation-12606581http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/12606581