Evidence map›Paper›PMID 23778362›Full record

ArticleMolecular pharmacology2013

Segregation of family A G protein-coupled receptor protomers in the plasma membrane.

Anthony Gavalas, Tien-Hung Lan, Qiuju Liu, Ivan R Corrêa, Jonathan A Javitch, Nevin A Lambert

Open access · bronzeAbstract read
In one paragraph

Article in Molecular pharmacology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

15 citing papers in PubMed, 29 citations in OpenAlex.

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  13. Family a GPCR heteromers in animal models.Frontiers in pharmacology · 2014
    Article
  14. Review
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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

6 authors at 3 institutions in 1 country.

Anthony GavalasDepartment of Pharmacology and Toxicology, Medical College of Georgia, Georgia Regents University, Augusta, Georgia 30912-2300, USA.
Tien-Hung Lan
Qiuju Liu
Ivan R Corrêa
Jonathan A Javitch
Nevin A Lambert
Columbia University · USAugusta University · USNew York Psychoanalytic Society and Institute · US

Funding

Structure of the Dopamine D2-Like Receptor Binding SitesR01MH054137 · NIMH · NEW YORK STATE PSYCHIATRIC INSTITUTE DBA RESEARCH FOUNDATION FOR MENTAL HYGIENE, INC · PI JAVITCH, JONATHAN A · 1995 to 2025
$12.0M
GPCR signaling complexes in living cellsR01GM078319 · NIGMS · AUGUSTA UNIVERSITY · PI LAMBERT, NEVIN ALAN · 2007 to 2017
$2.1M
Molecular Determinants for the Action of PsychostimulantsK05DA022413 · NIDA · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI JAVITCH, JONATHAN A · 2007 to 2016
$1.3M
Hydrophobic mismatch and self-association of TM proteins and beta2 adrenoreceptorR01GM096762 · NIGMS · AUGUSTA UNIVERSITY · PI LAMBERT, NEVIN ALAN · 2011 to 2012
$373k
NIDA NIH HHS DA022413NIDA NIH HHS K05 DA022413NIGMS NIH HHS GM078319NIGMS NIH HHS GM096762NIGMS NIH HHS R01 GM078319NIGMS NIH HHS R01 GM096762NIMH NIH HHS MH54137NIMH NIH HHS R01 MH054137
6 · The paper itself

Abstract

G protein-coupled receptors (GPCRs) transduce many important physiological signals and are targets for a large fraction of therapeutic drugs. Members of the largest family of GPCRs (family A) are thought to self-associate as dimers and higher-order oligomers, although the significance of such quaternary structures for signaling or receptor trafficking is known for only a few examples. One outstanding question is the physical stability of family A oligomers in cell membranes. Stable oligomers would be expected to move through cellular compartments and membrane domains as intact groups of protomers. Here, we test this prediction by recruiting subsets of affinity-tagged family A protomers into artificial microdomains on the surface of living cells and asking if untagged protomers move into these domains (are corecruited) at the same time. We find that tagged β₂ adrenergic and μ-opioid protomers are unable to corecruit untagged protomers into microdomains. In contrast, tagged metabotropic glutamate receptor protomers do corecruit untagged protomers into such microdomains, which is consistent with the known covalent mechanism whereby these family C receptors dimerize. These observations suggest that interactions between these family A protomers are too weak to directly influence subcellular location, and that mechanisms that move these receptors between subcellular compartments and domains must operate on individual protomers.

Indexed as

Promoter Regions, GeneticAnimalsCell MembraneChlorocebus aethiopsCHO CellsCOS CellsCricetinaeCricetulusHEK293 CellsHumansMembrane MicrodomainsProtein MultimerizationProtein TransportReceptors, Adrenergic, beta-2Receptors, Opioid, muReceptors, Adrenergic, beta-2Receptors, Opioid, mu

Identifiers

PMID23778362
PMCPMC3876820
OpenAlexW2108376144

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.