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• W2099358486 abstract "Ubiquitination of the human κ opioid receptor (hKOR) expressed in Chinese hamster ovary (CHO) cells was observed in the presence of the proteasomal inhibitor <i>N</i>-benzoyloxycarbonyl (<i>Z</i>)-Leu-Leu-leucinal (MG132) and enhanced by the agonists (-)(<i>trans</i>)-3,4-dichloro-<i>N</i>-methyl-<i>N</i>-[2-(1-pyrrolidiny) cyclohexyl] benzeneacetamide (U50,488H) and dynorphin A (Dyn A). The dominant-negative (DN) mutants GRK2-K220R and β-arrestin (319-418), but not dynamin I-K44A, reduced Dyn A-stimulated hKOR ubiquitination, and a phosphorylation-defective hKOR mutant (hKOR-S358N) did not undergo Dyn A-stimulated ubiquitination, indicating that hKOR ubiquitination is enhanced by receptor phosphorylation but not by receptor internalization. A hKOR mutant (hKOR-10 KR) in which all 10 intracellular Lys residues were changed to Arg showed greatly reduced basal and agonist-promoted receptor ubiquitination and substantially decreased Dyn A-induced receptor down-regulation, without changing ligand binding affinity, receptor-G protein coupling, or receptor internalization or desensitization. The ubiquitination sites were further determined to be the three Lys residues in the C-terminal domain. The K63R ubiquitin mutant decreased Dyn A-induced hKOR ubiquitination and down-regulation, but the K48R mutant did not. Expression of HN-CYLD, a DN mutant of deubiquitination enzyme cylindromatosis tumor suppressor gene (CYLD) that breaks Lys63-linked polyubiquitin chain, increased Dyn A-induced hKOR ubiquitination and down-regulation. These results indicate that ubiquitinated hKOR after agonist treatment contains predominantly Lys63-linked polyubiquitin chains and ubiquitination of the hKOR involved in agonist-induced down-regulation." @default.
• W2099358486 created "2016-06-24" @default.
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• W2099358486 date "2008-01-22" @default.
• W2099358486 modified "2023-09-23" @default.
• W2099358486 title "Agonist-Promoted Lys63-Linked Polyubiquitination of the Human κ-Opioid Receptor Is Involved in Receptor Down-Regulation" @default.
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• W2099358486 doi "https://doi.org/10.1124/mol.107.042846" @default.
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