| RRC ID |
73442
|
| 著者 |
Miyoshi K, Shimizu S, Shiraki A, Egi M.
|
| タイトル |
Ubiquitination of the μ-opioid receptor regulates receptor internalization without affecting Gi/o-mediated intracellular signaling or receptor phosphorylation.
|
| ジャーナル |
Biochem Biophys Res Commun
|
| Abstract |
Opioids are highly potent analgesics but develop tolerance. Previous studies have focused on phosphorylation of the μ-opioid receptor as it is involved in maintaining cellular sensitivity via desensitization, recycling, and degradation of the activated receptor. Recently, ubiquitination, another form of posttranslational modification has attracted attention in terms of triggering intracellular signaling and regulation of the activated receptor. Here, we generated a ubiquitination-deficient mutant of the μ-opioid receptor to investigate whether ubiquitination is involved in driving Gi/o-mediated analgesic signaling, receptor desensitization or subsequent receptor internalization. Our study shows that the Gi/o pathway and receptor phosphorylation do not require ubiquitination. Instead, ubiquitination regulates the internalization efficiency and might help in promoting internalization of the desensitized MOP.
|
| 巻・号 |
643
|
| ページ |
96-104
|
| 公開日 |
2022-12-29
|
| DOI |
10.1016/j.bbrc.2022.12.077
|
| PII |
S0006-291X(22)01756-9
|
| PMID |
36592585
|
| MeSH |
Analgesics / pharmacology
Analgesics, Opioid / pharmacology
Morphine* / pharmacology
Phosphorylation
Receptors, Opioid, mu* / genetics
Receptors, Opioid, mu* / metabolism
Signal Transduction
Ubiquitination
|
| IF |
2.985
|
| リソース情報 |
| ヒト・動物細胞 |
293(RCB1637) |
| 遺伝子材料 |
CSII-CMV-MCS-IRES2-Bsd (RDB04385) |
