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http://purl.uniprot.org/citations/28169830http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/28169830http://www.w3.org/2000/01/rdf-schema#comment"In addition to their role in desensitization and internalization of G protein-coupled receptors (GPCRs), β-arrestins are essential scaffolds linking GPCRs to Erk1/2 signaling. However, their role in GPCR-operated Erk1/2 activation differs between GPCRs and the underlying mechanism remains poorly characterized. Here, we show that activation of serotonin 5-HT2C receptors, which engage Erk1/2 pathway via a β-arrestin-dependent mechanism, promotes MEK-dependent β-arrestin2 phosphorylation at Thr383, a necessary step for Erk recruitment to the receptor/β-arrestin complex and Erk activation. Likewise, Thr383 phosphorylation is involved in β-arrestin-dependent Erk1/2 stimulation elicited by other GPCRs such as β2-adrenergic, FSH and CXCR4 receptors, but does not affect the β-arrestin-independent Erk1/2 activation by 5-HT4 receptor. Collectively, these data show that β-arrestin2 phosphorylation at Thr383 underlies β-arrestin-dependent Erk1/2 activation by GPCRs."xsd:string
http://purl.uniprot.org/citations/28169830http://purl.org/dc/terms/identifier"doi:10.7554/elife.23777"xsd:string
http://purl.uniprot.org/citations/28169830http://purl.uniprot.org/core/author"Bockaert J."xsd:string
http://purl.uniprot.org/citations/28169830http://purl.uniprot.org/core/author"Cassier E."xsd:string
http://purl.uniprot.org/citations/28169830http://purl.uniprot.org/core/author"Claeysen S."xsd:string
http://purl.uniprot.org/citations/28169830http://purl.uniprot.org/core/author"Marin P."xsd:string
http://purl.uniprot.org/citations/28169830http://purl.uniprot.org/core/author"Reiter E."xsd:string
http://purl.uniprot.org/citations/28169830http://purl.uniprot.org/core/author"Vandermoere F."xsd:string
http://purl.uniprot.org/citations/28169830http://purl.uniprot.org/core/author"Poupon A."xsd:string
http://purl.uniprot.org/citations/28169830http://purl.uniprot.org/core/author"Crepieux P."xsd:string
http://purl.uniprot.org/citations/28169830http://purl.uniprot.org/core/author"Gallay N."xsd:string
http://purl.uniprot.org/citations/28169830http://purl.uniprot.org/core/author"Bourquard T."xsd:string
http://purl.uniprot.org/citations/28169830http://purl.uniprot.org/core/date"2017"xsd:gYear
http://purl.uniprot.org/citations/28169830http://purl.uniprot.org/core/name"Elife"xsd:string
http://purl.uniprot.org/citations/28169830http://purl.uniprot.org/core/pages"e23777"xsd:string
http://purl.uniprot.org/citations/28169830http://purl.uniprot.org/core/title"Phosphorylation of beta-arrestin2 at Thrpisup>383pi/sup> by MEK underlies beta-arrestin-dependent activation of Erk1/2 by GPCRs."xsd:string
http://purl.uniprot.org/citations/28169830http://purl.uniprot.org/core/volume"6"xsd:string
http://purl.uniprot.org/citations/28169830http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/28169830
http://purl.uniprot.org/citations/28169830http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/28169830
http://purl.uniprot.org/uniprot/#_A1QJE5-mappedCitation-28169830http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/28169830
http://purl.uniprot.org/uniprot/#_A8K4I6-mappedCitation-28169830http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/28169830
http://purl.uniprot.org/uniprot/#_B4DHN0-mappedCitation-28169830http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/28169830
http://purl.uniprot.org/uniprot/#_L7RXH5-mappedCitation-28169830http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/28169830
http://purl.uniprot.org/uniprot/#_K7ENA6-mappedCitation-28169830http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/28169830