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http://purl.uniprot.org/citations/16314496http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16314496http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16314496http://www.w3.org/2000/01/rdf-schema#comment"The TRAP/Mediator coactivator complex serves as a molecular bridge between gene-specific activators and RNA polymerase II. TRAP220/Med1 is a key component of TRAP/Mediator that targets the complex to nuclear hormone receptors and other types of activators. We show here that human TRAP220/Med1 is a specific substrate for extracellular signal-regulated kinase (ERK) of the mitogen-activated protein kinase (MAPK) family. We demonstrate that ERK phosphorylates TRAP220/Med1 in vivo at two specific sites: threonine 1032 and threonine 1457. Importantly, we found that ERK phosphorylation significantly increases the stability and half-life of TRAP220/Med1 in vivo and correlates with increased thyroid hormone receptor-dependent transcription. Furthermore, ERK phosphorylates TRAP220/Med1 in a cell cycle-dependent manner, resulting in peak levels of expression during the G(2)/M phase of the cell cycle. ERK phosphorylation of ectopic TRAP220/Med1 also triggered shuttling into the nucleolus, thus suggesting that ERK may regulate TRAP220/Med1 subnuclear localization. Finally, we observed that ERK phosphorylation of TRAP220/Med1 stimulates its intrinsic transcriptional coactivation activity. We propose that ERK-mediated phosphorylation is a regulatory mechanism that controls TRAP220/Med1 expression levels and modulates its functional activity."xsd:string
http://purl.uniprot.org/citations/16314496http://purl.org/dc/terms/identifier"doi:10.1128/mcb.25.24.10695-10710.2005"xsd:string
http://purl.uniprot.org/citations/16314496http://purl.org/dc/terms/identifier"doi:10.1128/mcb.25.24.10695-10710.2005"xsd:string
http://purl.uniprot.org/citations/16314496http://purl.uniprot.org/core/author"Lin X."xsd:string
http://purl.uniprot.org/citations/16314496http://purl.uniprot.org/core/author"Lin X."xsd:string
http://purl.uniprot.org/citations/16314496http://purl.uniprot.org/core/author"Sharma D."xsd:string
http://purl.uniprot.org/citations/16314496http://purl.uniprot.org/core/author"Sharma D."xsd:string
http://purl.uniprot.org/citations/16314496http://purl.uniprot.org/core/author"Fondell J.D."xsd:string
http://purl.uniprot.org/citations/16314496http://purl.uniprot.org/core/author"Fondell J.D."xsd:string
http://purl.uniprot.org/citations/16314496http://purl.uniprot.org/core/author"Shapiro P.S."xsd:string
http://purl.uniprot.org/citations/16314496http://purl.uniprot.org/core/author"Shapiro P.S."xsd:string
http://purl.uniprot.org/citations/16314496http://purl.uniprot.org/core/author"Pandey P.K."xsd:string
http://purl.uniprot.org/citations/16314496http://purl.uniprot.org/core/author"Pandey P.K."xsd:string
http://purl.uniprot.org/citations/16314496http://purl.uniprot.org/core/author"Udayakumar T.S."xsd:string
http://purl.uniprot.org/citations/16314496http://purl.uniprot.org/core/author"Udayakumar T.S."xsd:string
http://purl.uniprot.org/citations/16314496http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/16314496http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/16314496http://purl.uniprot.org/core/name"Mol. Cell. Biol."xsd:string
http://purl.uniprot.org/citations/16314496http://purl.uniprot.org/core/name"Mol. Cell. Biol."xsd:string
http://purl.uniprot.org/citations/16314496http://purl.uniprot.org/core/pages"10695-10710"xsd:string
http://purl.uniprot.org/citations/16314496http://purl.uniprot.org/core/pages"10695-10710"xsd:string
http://purl.uniprot.org/citations/16314496http://purl.uniprot.org/core/title"Activation of TRAP/mediator subunit TRAP220/Med1 is regulated by mitogen-activated protein kinase-dependent phosphorylation."xsd:string
http://purl.uniprot.org/citations/16314496http://purl.uniprot.org/core/title"Activation of TRAP/mediator subunit TRAP220/Med1 is regulated by mitogen-activated protein kinase-dependent phosphorylation."xsd:string