Evidence map›Paper›PMID 32541966›Full record

ArticleNature chemical biology2020

Single-molecule analysis reveals agonist-specific dimer formation of µ-opioid receptors.

Jan Möller, Ali Isbilir, Titiwat Sungkaworn, Brendan Osberg, Christos Karathanasis, Vikram Sunkara, Eugene O Grushevskyi, Andreas Bock, Paolo Annibale, Mike Heilemann and 2 more

Abstract read
PubMed Publisher
In one paragraph

Article in Nature chemical biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed
6.8field-weighted citation impact, top 2% 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

66 citing papers in PubMed, 125 citations in OpenAlex.

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  16. Physics-informed deep learning for stochastic particle dynamics estimation.Proceedings of the National Academy of Sciences of the United States of America · 2025
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  17. Higher-order transient membrane protein structures.Proceedings of the National Academy of Sciences of the United States of America · 2025
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  18. Article
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  20. Article

6 more citing papers are in PubMed but not listed here.

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

12 authors at 4 institutions in 2 countries.

Jan MöllerMax Delbrück Center for Molecular Medicine, Berlin, Germany.ORCID http://orcid.org/0000-0001-8429-3784
Ali IsbilirMax Delbrück Center for Molecular Medicine, Berlin, Germany.
Titiwat SungkawornInstitute of Pharmacology and Toxicology, University of Würzburg, Würzburg, Germany.
Brendan OsbergMax Delbrück Center for Molecular Medicine, Berlin, Germany.
Christos KarathanasisInstitute of Physical and Theoretical Chemistry, Goethe-University Frankfurt, Frankfurt, Germany.
Vikram SunkaraZuse Institute Berlin, Berlin, Germany.
Eugene O GrushevskyiMax Delbrück Center for Molecular Medicine, Berlin, Germany.ORCID http://orcid.org/0000-0003-1779-8306
Andreas BockMax Delbrück Center for Molecular Medicine, Berlin, Germany.ORCID http://orcid.org/0000-0002-6344-6494
Paolo AnnibaleMax Delbrück Center for Molecular Medicine, Berlin, Germany.ORCID http://orcid.org/0000-0003-3208-5347
Mike HeilemannInstitute of Physical and Theoretical Chemistry, Goethe-University Frankfurt, Frankfurt, Germany.ORCID http://orcid.org/0000-0002-9821-3578
Christof SchütteZuse Institute Berlin, Berlin, Germany.
Martin J LohseMax Delbrück Center for Molecular Medicine, Berlin, Germany. m.lohse@mdc-berlin.de.
Max Delbrück Center · DEGoethe University Frankfurt · DEZuse Institute Berlin · DEMahidol University · TH

Funding

Biophysical approaches to investigate the biological significance of GPCR dimersR01DA038882 · NIDA · ICAHN SCHOOL OF MEDICINE AT MOUNT SINAI · PI FILIZOLA, MARTA · 2015 to 2019
$1.7M
NIDA NIH HHS R01 DA038882
6 · The paper itself

Abstract

G-protein-coupled receptors (GPCRs) are key signaling proteins that mostly function as monomers, but for several receptors constitutive dimer formation has been described and in some cases is essential for function. Using single-molecule microscopy combined with super-resolution techniques on intact cells, we describe here a dynamic monomer-dimer equilibrium of µ-opioid receptors (µORs), where dimer formation is driven by specific agonists. The agonist DAMGO, but not morphine, induces dimer formation in a process that correlates both temporally and in its agonist- and phosphorylation-dependence with β-arrestin2 binding to the receptors. This dimerization is independent from, but may precede, µOR internalization. These data suggest a new level of GPCR regulation that links dimer formation to specific agonists and their downstream signals.

Indexed as

Animalsbeta-ArrestinsCHO CellsCricetulusEnkephalin, Ala(2)-MePhe(4)-Gly(5)-Fluorescence Resonance Energy TransferMorphineMutationNaloxoneNaltrexoneNarcotic AntagonistsPhosphorylationProtein MultimerizationReceptors, Opioid, muSingle Molecule Imagingbeta-Arrestinsbeta-funaltrexamineEnkephalin, Ala(2)-MePhe(4)-Gly(5)-MorphineNaloxoneNaltrexoneNarcotic AntagonistsReceptors, Opioid, mu

Identifiers

PMID32541966
OpenAlexW3034718462

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.