| http://purl.uniprot.org/citations/15166223 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15166223 | http://www.w3.org/2000/01/rdf-schema#comment | "Class II histone deacetylases (HDACs) play a role in myogenesis and inhibit transcriptional activation by myocyte enhancer factors 2. A distinct feature of class II HDACs is their ability to shuttle between the nucleus and the cytoplasm in a cell type- and signal-dependent manner. We demonstrate here that treatment with the 26 S proteosome inhibitors, MG132 and ALLN, leads to detection of ubiquitinated HDAC7 and causes accumulation of cytoplasmic HDAC7. We also show that treatment with calyculin A, a protein phosphatase inhibitor, leads to a marked increase of HDAC7 but not HDAC5. The increase in HDAC7 is accompanied by enhanced interaction between 14-3-3 proteins and HDAC7. HDAC7 mutations that prevent the interaction with 14-3-3 proteins also block calyculin A-mediated stabilization. Expression of constitutively active calcium/calmodulin-dependent kinase I stabilizes HDAC7 and causes an increased association between HDAC7 and 14-3-3. Together, our results suggest that calcium/calmodulin-dependent kinase I-mediated phosphorylation of HDAC7 acts, in part, to promote association of HDAC7 with 14-3-3 and stabilizes HDAC7."xsd:string |
| http://purl.uniprot.org/citations/15166223 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m405179200"xsd:string |
| http://purl.uniprot.org/citations/15166223 | http://purl.uniprot.org/core/author | "Liu Y."xsd:string |
| http://purl.uniprot.org/citations/15166223 | http://purl.uniprot.org/core/author | "Li X."xsd:string |
| http://purl.uniprot.org/citations/15166223 | http://purl.uniprot.org/core/author | "Song S."xsd:string |
| http://purl.uniprot.org/citations/15166223 | http://purl.uniprot.org/core/author | "Ko S.H."xsd:string |
| http://purl.uniprot.org/citations/15166223 | http://purl.uniprot.org/core/author | "Kao H.Y."xsd:string |
| http://purl.uniprot.org/citations/15166223 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
| http://purl.uniprot.org/citations/15166223 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/15166223 | http://purl.uniprot.org/core/pages | "34201-34208"xsd:string |
| http://purl.uniprot.org/citations/15166223 | http://purl.uniprot.org/core/title | "Phosphorylation of the histone deacetylase 7 modulates its stability and association with 14-3-3 proteins."xsd:string |
| http://purl.uniprot.org/citations/15166223 | http://purl.uniprot.org/core/volume | "279"xsd:string |
| http://purl.uniprot.org/citations/15166223 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/15166223 |
| http://purl.uniprot.org/citations/15166223 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/15166223 |
| http://purl.uniprot.org/uniprot/#_E9PZG4-mappedCitation-15166223 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/15166223 |
| http://purl.uniprot.org/uniprot/#_E9PX62-mappedCitation-15166223 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/15166223 |
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| http://purl.uniprot.org/uniprot/#_F6RY11-mappedCitation-15166223 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/15166223 |
| http://purl.uniprot.org/uniprot/#_F6WA09-mappedCitation-15166223 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/15166223 |
| http://purl.uniprot.org/uniprot/#_Q1EDY4-mappedCitation-15166223 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/15166223 |
| http://purl.uniprot.org/uniprot/#_Q1EDY5-mappedCitation-15166223 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/15166223 |