Evidence map›Paper›PMID 23106126›Full record

ArticleJournal of neurochemistry2013

Identification of phosphorylation sites in the COOH-terminal tail of the μ-opioid receptor.

Ying-Ju Chen, Sue Oldfield, Adrian J Butcher, Andrew B Tobin, Kunal Saxena, Vsevolod V Gurevich, Jeffrey L Benovic, Graeme Henderson, Eamonn Kelly

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in Journal of neurochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
2.6field-weighted citation impact, top 11% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

32 citing papers in PubMed, 43 citations in OpenAlex.

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  12. A cellular perspective of bias at G protein-coupled receptors.Protein science : a publication of the Protein Society · 2020
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors at 4 institutions in 2 countries.

Ying-Ju ChenSchool of Physiology and Pharmacology, University of Bristol, Bristol, UK.
Sue Oldfield
Adrian J Butcher
Andrew B Tobin
Kunal Saxena
Vsevolod V Gurevich
Jeffrey L Benovic
Graeme Henderson
Eamonn Kelly
University of Bristol · GBUniversity of Leicester · GBThomas Jefferson University · USVanderbilt University Medical Center · US

Funding

Arrestin interactions with non-receptor binding partnersR01GM077561 · NIGMS · VANDERBILT UNIVERSITY · PI GUREVICH, VSEVOLOD V. · 2007 to 2015
$2.3M
Medical Research Council G1100712Medical Research Council MR/J013269/1NIGMS NIH HHS GM077561NIGMS NIH HHS R01 GM077561
6 · The paper itself

Abstract

Phosphorylation is considered a key event in the signalling and regulation of the μ opioid receptor (MOPr). Here, we used mass spectroscopy to determine the phosphorylation status of the C-terminal tail of the rat MOPr expressed in human embryonic kidney 293 (HEK-293) cells. Under basal conditions, MOPr is phosphorylated on Ser(363) and Thr(370), while in the presence of morphine or [D-Ala2, NMe-Phe4, Gly-ol5]-enkephalin (DAMGO), the COOH terminus is phosphorylated at three additional residues, Ser(356) , Thr(357) and Ser(375). Using N-terminal glutathione S transferase (GST) fusion proteins of the cytoplasmic, C-terminal tail of MOPr and point mutations of the same, we show that, in vitro, purified G protein-coupled receptor kinase 2 (GRK2) phosphorylates Ser(375), protein kinase C (PKC) phosphorylates Ser(363), while CaMKII phosphorylates Thr(370). Phosphorylation of the GST fusion protein of the C-terminal tail of MOPr enhanced its ability to bind arrestin-2 and -3. Hence, our study identifies both the basal and agonist-stimulated phospho-acceptor sites in the C-terminal tail of MOPr, and suggests that the receptor is subject to phosphorylation and hence regulation by multiple protein kinases.

Indexed as

5' Flanking RegionAmino Acid SequenceAnimalsHEK293 CellsHumansMolecular Sequence DataPhosphorylationProtein KinasesProtein Structure, TertiaryProtein TransportRatsReceptors, Opioid, muProtein KinasesReceptors, Opioid, mu

Identifiers

PMID23106126
PMCPMC4226418
OpenAlexW1972379135

What OpenQuestion holds

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.