Evidence map›Paper›PMID 23798571›Full record

ArticleMolecular endocrinology (Baltimore, Md.)2013

Novel, gel-free proteomics approach identifies RNF5 and JAMP as modulators of GPCR stability.

Sébastien J Roy, Irina Glazkova, Louis Fréchette, Christian Iorio-Morin, Chantal Binda, Darlaine Pétrin, Phan Trieu, Mélanie Robitaille, Stéphane Angers, Terence E Hébert and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in Molecular endocrinology (Baltimore, Md.), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

24 citing papers in PubMed, 34 citations in OpenAlex.

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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

11 authors at 3 institutions in 1 country.

Sébastien J RoyService de Rhumatologie Département de Médecine, Université de Sherbrooke, the Institut de Pharmacologie de Sherbrooke, and the Centre de Recherche Clinique Etienne-Lebel, Sherbrooke, Québec J1H 5N4, Canada.
Irina Glazkova
Louis Fréchette
Christian Iorio-Morin
Chantal Binda
Darlaine Pétrin
Phan Trieu
Mélanie Robitaille
Stéphane Angers
Terence E Hébert
Jean-Luc Parent
Université de Sherbrooke · CAMcGill University · CAUniversity of Toronto · CA

Funding

Canadian Institutes of Health Research
6 · The paper itself

Abstract

The maturation and folding of G protein-coupled receptors are governed by mechanisms that remain poorly understood. In an effort to characterize these biological events, we optimized a novel, gel-free proteomic approach to identify partners of the β2-adrenergic receptor (β2AR). In addition to a number of known interacting proteins such as heterotrimeric G protein subunits, this allowed us to identify proteins involved in endoplasmic reticulum (ER) QC of the receptor. Among β2AR-associated proteins is Ring finger protein 5 (RNF5), an E3 ubiquitin ligase anchored to the outer membrane of the ER. Coimmunoprecipitation assays confirmed, in a cellular context, the interaction between RNF5 and the β2AR as well as the prostaglandin D2 receptor (DP). Confocal microscopy revealed that DP colocalized with RNF5 at the ER. Coexpression of RNF5 with either receptor increased levels of their expression, whereas small interfering RNA-mediated knockdown of endogenous RNF5 promoted the opposite. RNF5 did not modulate the ubiquitination state of β2AR or DP. Instead, RNF5 ubiquitinated JNK-associated membrane protein (JAMP), a protein that recruits the proteasome to the ER membrane and that is negatively regulated by RNF5-mediated ubiquitination. JAMP coimmunoprecipitated with both β2AR and DP and decreased total receptor protein levels through proteasomal degradation. Expression of DP, a receptor largely retained in the ER, promoted proteasome recruitment by JAMP. Degradation of both receptors via JAMP was increased when RNF5 was depleted. Our data suggest that RNF5 regulates the turnover of specific G protein-coupled receptors by ubiquitinating JAMP and preventing proteasome recruitment.

Indexed as

Carrier ProteinsCell LineDNA-Binding ProteinsEndoplasmic ReticulumHEK293 CellsHumansMembrane GlycoproteinsProteasome Endopeptidase ComplexProtein TransportProteomicsReceptors, Adrenergic, beta-2Receptors, ImmunologicReceptors, ProstaglandinRNA InterferenceRNA, Small InterferingSignal TransductionCarrier ProteinsDNA-Binding ProteinsJKAMP protein, humanMembrane Glycoproteinsprostaglandin D2 receptorProteasome Endopeptidase ComplexReceptors, Adrenergic, beta-2Receptors, ImmunologicReceptors, ProstaglandinRNA, Small InterferingRNF5 protein, humanUbiquitin-Protein Ligases

Identifiers

PMID23798571
PMCPMC5427950
OpenAlexW1970974117

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.