| http://purl.uniprot.org/citations/17698952 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/17698952 | http://www.w3.org/2000/01/rdf-schema#comment | "The endocannabinoid 2-arachidonoylglycerol (2-AG) enhances cell migration through the CB2 cannabinoid receptor. In this study, using an immunoprecipitation and mass spectrometry-based proteomic approach, we first identified the 90-kDa heat shock protein (Hsp90), a chaperone protein with novel signaling functions, as a CB2-interacting protein. The CB2/Hsp90 interaction was confirmed in human embryonic kidney 293 cells expressing transfected CB2 and in differentiated HL-60 cells expressing endogenous CB2, by coimmunoprecipitation and Western blot experiments, as well as by treatment with geldanamycin (GA), a specific Hsp90 inhibitor. Disruption of the CB2/Hsp90 interaction by treatment with GA or reducing Hsp90 levels with specific short interfering RNAs markedly inhibited 2-AG-induced cell migration, demonstrating that Hsp90 is crucial for 2-AG-induced cell migration. 2-AG treatment resulted in a CB2-mediated stimulation of Rac1 activity, and treatment with GA blocked 2AG-induced activation of Rac1. It is noteworthy that expression of the dominant-negative form of Rac1 reduced 2-AG-induced cell migration. These data demonstrate that 2-AG-induced activation of Rac1 is essential for 2-AG-induced cell migration, and the CB2/Hsp90 interaction is needed for 2-AG-induced activation of Rac1. Furthermore, 2-AG-induced Rac1 activation was sensitive to pertussis toxin treatment, hence involving G(i) proteins. In addition, treatment with GA significantly inhibited the CB2/Galpha(i2) interaction. As a whole, our data indicate that Hsp90 may serve as scaffold to keep the CB2 receptor and its signaling components, including Galpha(i2), in proximity, thus facilitating CB2-mediated signaling to cell migration through the G(i)-Rac1 pathway. By demonstrating that Hsp90 is essential for CB2-mediated signaling to cell migration, this study reveals a novel role of Hsp90 in the signaling events mediated by a G protein-coupled receptor."xsd:string |
| http://purl.uniprot.org/citations/17698952 | http://purl.org/dc/terms/identifier | "doi:10.1124/mol.107.036566"xsd:string |
| http://purl.uniprot.org/citations/17698952 | http://purl.uniprot.org/core/author | "He F."xsd:string |
| http://purl.uniprot.org/citations/17698952 | http://purl.uniprot.org/core/author | "Cai J."xsd:string |
| http://purl.uniprot.org/citations/17698952 | http://purl.uniprot.org/core/author | "Song Z.H."xsd:string |
| http://purl.uniprot.org/citations/17698952 | http://purl.uniprot.org/core/author | "He D.C."xsd:string |
| http://purl.uniprot.org/citations/17698952 | http://purl.uniprot.org/core/author | "Pierce W."xsd:string |
| http://purl.uniprot.org/citations/17698952 | http://purl.uniprot.org/core/author | "Qiao Z.H."xsd:string |
| http://purl.uniprot.org/citations/17698952 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |
| http://purl.uniprot.org/citations/17698952 | http://purl.uniprot.org/core/name | "Mol Pharmacol"xsd:string |
| http://purl.uniprot.org/citations/17698952 | http://purl.uniprot.org/core/pages | "1289-1300"xsd:string |
| http://purl.uniprot.org/citations/17698952 | http://purl.uniprot.org/core/title | "Involvement of the 90-kDa heat shock protein (Hsp-90) in CB2 cannabinoid receptor-mediated cell migration: a new role of Hsp-90 in migration signaling of a G protein-coupled receptor."xsd:string |
| http://purl.uniprot.org/citations/17698952 | http://purl.uniprot.org/core/volume | "72"xsd:string |
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