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http://purl.uniprot.org/citations/19363159http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19363159http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19363159http://www.w3.org/2000/01/rdf-schema#comment"Beta-arrestins are multifunctional adaptors that mediate the desensitization, internalization, and some signaling functions of seven-transmembrane receptors (7TMRs). Agonist-stimulated ubiquitination of beta-arrestin2 mediated by the E3 ubiquitin ligase Mdm2 is critical for rapid beta(2)-adrenergic receptor (beta(2)AR) internalization. We now report the discovery that the deubiquitinating enzyme ubiquitin-specific protease 33 (USP33) binds beta-arrestin2 and leads to the deubiquitination of beta-arrestins. USP33 and Mdm2 function reciprocally and favor respectively the stability or lability of the receptor beta-arrestin complex, thus regulating the longevity and subcellular localization of receptor signalosomes. Receptors such as the beta(2)AR, previously shown to form loose complexes with beta-arrestin ("class A") promote a beta-arrestin conformation conducive for binding to the deubiquitinase, whereas the vasopressin V2R, which forms tight beta-arrestin complexes ("class B"), promotes a distinct beta-arrestin conformation that favors dissociation of the enzyme. Thus, USP33-beta-arrestin interaction is a key regulatory step in 7TMR trafficking and signal transmission from the activated receptors to downstream effectors."xsd:string
http://purl.uniprot.org/citations/19363159http://purl.org/dc/terms/identifier"doi:10.1073/pnas.0901083106"xsd:string
http://purl.uniprot.org/citations/19363159http://purl.org/dc/terms/identifier"doi:10.1073/pnas.0901083106"xsd:string
http://purl.uniprot.org/citations/19363159http://purl.uniprot.org/core/author"Lefkowitz R.J."xsd:string
http://purl.uniprot.org/citations/19363159http://purl.uniprot.org/core/author"Lefkowitz R.J."xsd:string
http://purl.uniprot.org/citations/19363159http://purl.uniprot.org/core/author"Shukla A.K."xsd:string
http://purl.uniprot.org/citations/19363159http://purl.uniprot.org/core/author"Shukla A.K."xsd:string
http://purl.uniprot.org/citations/19363159http://purl.uniprot.org/core/author"Ahn S."xsd:string
http://purl.uniprot.org/citations/19363159http://purl.uniprot.org/core/author"Ahn S."xsd:string
http://purl.uniprot.org/citations/19363159http://purl.uniprot.org/core/author"Berthouze M."xsd:string
http://purl.uniprot.org/citations/19363159http://purl.uniprot.org/core/author"Berthouze M."xsd:string
http://purl.uniprot.org/citations/19363159http://purl.uniprot.org/core/author"Miller W.E."xsd:string
http://purl.uniprot.org/citations/19363159http://purl.uniprot.org/core/author"Miller W.E."xsd:string
http://purl.uniprot.org/citations/19363159http://purl.uniprot.org/core/author"Shenoy S.K."xsd:string
http://purl.uniprot.org/citations/19363159http://purl.uniprot.org/core/author"Shenoy S.K."xsd:string
http://purl.uniprot.org/citations/19363159http://purl.uniprot.org/core/author"Xiao K."xsd:string
http://purl.uniprot.org/citations/19363159http://purl.uniprot.org/core/author"Xiao K."xsd:string
http://purl.uniprot.org/citations/19363159http://purl.uniprot.org/core/author"Wilkinson K.D."xsd:string
http://purl.uniprot.org/citations/19363159http://purl.uniprot.org/core/author"Wilkinson K.D."xsd:string
http://purl.uniprot.org/citations/19363159http://purl.uniprot.org/core/author"Modi A.S."xsd:string
http://purl.uniprot.org/citations/19363159http://purl.uniprot.org/core/author"Modi A.S."xsd:string
http://purl.uniprot.org/citations/19363159http://purl.uniprot.org/core/date"2009"xsd:gYear
http://purl.uniprot.org/citations/19363159http://purl.uniprot.org/core/date"2009"xsd:gYear