| http://purl.uniprot.org/citations/24807909 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/24807909 | http://www.w3.org/2000/01/rdf-schema#comment | "The G protein-coupled receptor (GPCR) kinases (GRKs) phosphorylate activated GPCRs at the plasma membrane (PM). Here GRK5/GRK4 chimeras and point mutations in GRK5 identify a short sequence within the regulator of G protein signaling (RGS) domain in GRK5 that is critical for GRK5 PM localization. This region of the RGS domain of GRK5 coincides with a region of GRK6 and GRK1 shown to form a hydrophobic dimeric interface (HDI) in crystal structures. Coimmunoprecipitation (coIP) and acceptor photobleaching fluorescence resonance energy transfer assays show that expressed GRK5 self-associates in cells, whereas GRK5-M165E/F166E (GRK5-EE), containing hydrophilic mutations in the HDI region of the RGS domain, displays greatly decreased coIP interactions. Both forcing dimerization of GRK5-EE, via fusion to leucine zipper motifs, and appending an extra C-terminal membrane-binding region to GRK5-EE (GRK5-EE-CT) recover PM localization. In addition, GRK5-EE displays a decreased ability to inhibit PAR1-induced calcium release compared with GRK5 wild type (wt). In contrast, PM-localized GRK5-EE-CaaX (appending a C-terminal prenylation and polybasic motif from K-ras) or GRK5-EE-CT shows comparable ability to GRK5 wt to inhibit PAR1-induced calcium release. The results suggest a novel model in which GRK5 dimerization is important for its plasma membrane localization and function."xsd:string |
| http://purl.uniprot.org/citations/24807909 | http://purl.org/dc/terms/identifier | "doi:10.1091/mbc.e13-09-0547"xsd:string |
| http://purl.uniprot.org/citations/24807909 | http://purl.uniprot.org/core/author | "Jiang X."xsd:string |
| http://purl.uniprot.org/citations/24807909 | http://purl.uniprot.org/core/author | "Xu H."xsd:string |
| http://purl.uniprot.org/citations/24807909 | http://purl.uniprot.org/core/author | "Shen K."xsd:string |
| http://purl.uniprot.org/citations/24807909 | http://purl.uniprot.org/core/author | "Wedegaertner P.B."xsd:string |
| http://purl.uniprot.org/citations/24807909 | http://purl.uniprot.org/core/author | "Fischer C.C."xsd:string |
| http://purl.uniprot.org/citations/24807909 | http://purl.uniprot.org/core/date | "2014"xsd:gYear |
| http://purl.uniprot.org/citations/24807909 | http://purl.uniprot.org/core/name | "Mol Biol Cell"xsd:string |
| http://purl.uniprot.org/citations/24807909 | http://purl.uniprot.org/core/pages | "2105-2115"xsd:string |
| http://purl.uniprot.org/citations/24807909 | http://purl.uniprot.org/core/title | "The regulator of G protein signaling (RGS) domain of G protein-coupled receptor kinase 5 (GRK5) regulates plasma membrane localization and function."xsd:string |
| http://purl.uniprot.org/citations/24807909 | http://purl.uniprot.org/core/volume | "25"xsd:string |
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