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http://purl.uniprot.org/citations/11114197http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11114197http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11114197http://www.w3.org/2000/01/rdf-schema#comment"Skeletal muscle differentiation is controlled by interactions between myocyte enhancer factor-2 (MEF2) and myogenic basic helix-loop-helix transcription factors. Association of MEF2 with histone deacetylases (HDAC) -4 and -5 results in repression of MEF2 target genes and inhibition of myogenesis. Calcium/calmodulin-dependent protein kinase (CaMK) signaling promotes myogenesis by disrupting MEF2-HDAC complexes and stimulating HDAC nuclear export. To further define the mechanisms that confer CaMK responsiveness to HDAC4 and -5, we performed yeast two-hybrid screens to identify HDAC-interacting factors. These screens revealed interactions between HDAC4 and members of the 14-3-3 family of proteins, which function as signal-dependent intracellular chaperones. HDAC4 binds constitutively to 14-3-3 in yeast and mammalian cells, whereas HDAC5 binding to 14-3-3 is largely dependent on CaMK signaling. CaMK phosphorylates serines -259 and -498 in HDAC5, which subsequently serve as docking sites for 14-3-3. Our studies suggest that 14-3-3 binding to HDAC5 is required for CaMK-dependent disruption of MEF2-HDAC complexes and nuclear export of HDAC5, and implicate 14-3-3 as a signal-dependent regulator of muscle cell differentiation."xsd:string
http://purl.uniprot.org/citations/11114197http://purl.org/dc/terms/identifier"doi:10.1073/pnas.260501497"xsd:string
http://purl.uniprot.org/citations/11114197http://purl.org/dc/terms/identifier"doi:10.1073/pnas.260501497"xsd:string
http://purl.uniprot.org/citations/11114197http://purl.uniprot.org/core/author"Olson E.N."xsd:string
http://purl.uniprot.org/citations/11114197http://purl.uniprot.org/core/author"Olson E.N."xsd:string
http://purl.uniprot.org/citations/11114197http://purl.uniprot.org/core/author"Zhang C.-L."xsd:string
http://purl.uniprot.org/citations/11114197http://purl.uniprot.org/core/author"Zhang C.-L."xsd:string
http://purl.uniprot.org/citations/11114197http://purl.uniprot.org/core/author"McKinsey T.A."xsd:string
http://purl.uniprot.org/citations/11114197http://purl.uniprot.org/core/author"McKinsey T.A."xsd:string
http://purl.uniprot.org/citations/11114197http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/11114197http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/11114197http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/11114197http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/11114197http://purl.uniprot.org/core/pages"14400-14405"xsd:string
http://purl.uniprot.org/citations/11114197http://purl.uniprot.org/core/pages"14400-14405"xsd:string
http://purl.uniprot.org/citations/11114197http://purl.uniprot.org/core/title"Activation of the myocyte enhancer factor-2 transcription factor by calcium/calmodulin-dependent protein kinase-stimulated binding of 14-3-3 to histone deacetylase 5."xsd:string
http://purl.uniprot.org/citations/11114197http://purl.uniprot.org/core/title"Activation of the myocyte enhancer factor-2 transcription factor by calcium/calmodulin-dependent protein kinase-stimulated binding of 14-3-3 to histone deacetylase 5."xsd:string
http://purl.uniprot.org/citations/11114197http://purl.uniprot.org/core/volume"97"xsd:string
http://purl.uniprot.org/citations/11114197http://purl.uniprot.org/core/volume"97"xsd:string
http://purl.uniprot.org/citations/11114197http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11114197
http://purl.uniprot.org/citations/11114197http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11114197
http://purl.uniprot.org/citations/11114197http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/11114197
http://purl.uniprot.org/citations/11114197http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/11114197