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• W1520805737 abstract "The efficiency of μ‐opioid receptor signalling is tightly regulated and ultimately limited by the coordinated phosphorylation of intracellular serine and threonine residues. Here, we review and discuss recent progress in the generation and application of phosphosite‐specific μ‐opioid receptor antibodies, which have proved to be excellent tools for monitoring the spatial and temporal dynamics of receptor phosphorylation and dephosphorylation. Agonist‐induced phosphorylation of μ‐opioid receptors occurs at a conserved 10 residue sequence 370 TREHPSTANT 379 in the receptor's carboxyl‐terminal cytoplasmic tail. Diverse opioids induce receptor phosphorylation at S 375, present in the middle of this sequence, but only high‐efficacy opioids have the ability to drive higher order phosphorylation on flanking residues ( T 370, T 376 and T 379). S 375 is the initiating residue in a hierarchical phosphorylation cascade. In contrast, agonist‐independent heterologous μ‐opioid receptor phosphorylation occurs primarily at T 370. The combination of phosphosite‐specific antibodies and si RNA knockdown screening also facilitated the identification of relevant kinases and phosphatases. In fact, morphine induces a selective S 375 phosphorylation that is predominantly catalysed by GPCR kinase 5 ( GRK 5), whereas multisite phosphorylation induced by high‐efficacy opioids specifically requires GRK 2/3. By contrast, T 370 phosphorylation stimulated by phorbol esters or heterologous activation of G q ‐coupled receptors is mediated by PKC α. Rapid μ‐opioid receptor dephosphorylation occurs at or near the plasma membrane and is catalysed by protein phosphatase 1γ ( PP 1γ). These findings suggest that there are distinct phosphorylation motifs for homologous and heterologous regulation of μ‐opioid receptor phosphorylation. However, it remains to be seen to what extent different μ‐opioid receptor phosphorylation patterns contribute to the development of tolerance and dependence in vivo . Linked Articles This article is part of a themed section on Opioids: New Pathways to Functional Selectivity. To view the other articles in this section visit http://dx.doi.org/10.1111/bph.2015.172.issue-2" @default.
• W1520805737 created "2016-06-24" @default.
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• W1520805737 date "2014-07-01" @default.
• W1520805737 modified "2023-10-11" @default.
• W1520805737 title "Different mechanisms of homologous and heterologous μ‐opioid receptor phosphorylation" @default.
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• W1520805737 doi "https://doi.org/10.1111/bph.12627" @default.
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