Evidence map›Paper›PMID 40442125›Full record

ArticleNature communications2025

Lipids modulate the dynamics of GPCR:β-arrestin interaction.

Antoniel A S Gomes, Michela Di Michele, Rita Ann Roessner, Marjorie Damian, Paulo M Bisch, Nathalie Sibille, Maxime Louet, Jean-Louis Banères, Nicolas Floquet

Abstract read
In one paragraph

Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
–field-weighted citation impact
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

10 citing papers in PubMed.

  1. Article
  2. Review
  3. Factors modulating the assembly of human βNature structural & molecular biology · 2026
    Article
  4. The working lives of neuronal 5-HTRSC chemical biology · 2026
    Review
  5. Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Review
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.

Antoniel A S Gomes *Institut des Biomolécules Max Mousseron (IBMM), UMR 5247 CNRS, Université de Montpellier, ENSCM, Montpellier cedex 5, France.
Michela Di Michele *Institut des Biomolécules Max Mousseron (IBMM), UMR 5247 CNRS, Université de Montpellier, ENSCM, Montpellier cedex 5, France.ORCID http://orcid.org/0000-0002-0739-5004
Rita Ann RoessnerInstitut des Biomolécules Max Mousseron (IBMM), UMR 5247 CNRS, Université de Montpellier, ENSCM, Montpellier cedex 5, France.ORCID http://orcid.org/0009-0008-4575-9236
Marjorie DamianInstitut des Biomolécules Max Mousseron (IBMM), UMR 5247 CNRS, Université de Montpellier, ENSCM, Montpellier cedex 5, France.
Paulo M BischLaboratório de Física Biológica, Instituto de Biofísica Carlos Chagas Filho, Universidade Federal do, Rio de Janeiro, Brazil.
Nathalie SibilleCentre de Biologie Structurale (CBS), CNRS, Université de Montpellier, Inserm, Montpellier, France.ORCID http://orcid.org/0000-0001-8145-6795
Maxime LouetInstitut des Biomolécules Max Mousseron (IBMM), UMR 5247 CNRS, Université de Montpellier, ENSCM, Montpellier cedex 5, France.
Jean-Louis BanèresInstitut des Biomolécules Max Mousseron (IBMM), UMR 5247 CNRS, Université de Montpellier, ENSCM, Montpellier cedex 5, France.ORCID http://orcid.org/0000-0001-7078-1285
Nicolas FloquetInstitut des Biomolécules Max Mousseron (IBMM), UMR 5247 CNRS, Université de Montpellier, ENSCM, Montpellier cedex 5, France. nicolas.floquet@umontpellier.fr.ORCID http://orcid.org/0009-0006-6072-5363

Funding

Agence Nationale de la Recherche (French National Research Agency) ANR-20-CE92-0028Agence Nationale de la Recherche (French National Research Agency) ANR-21-CE29-0012
6 · The paper itself

Abstract

β-arrestins are key molecular partners of G Protein-Coupled Receptors (GPCRs), triggering not only their desensitization but also intracellular signaling. Existing structural data point to high conformational plasticity of GPCR:β-arrestin interaction, with two completely different orientations between receptor and β-arrestin. Combining molecular dynamics simulations and fluorescence spectroscopy, we show that β-arrestin 1 interacts with membranes even in the absence of a receptor, an interaction that is enhanced by PI(4,5)P2, presumably holding the β-arrestin 1 C-edge loop into the lipid bilayer. This key interaction helps β-arrestin 1 to adopt a "receptor-ready" orientation and consequently favors its coupling to the ghrelin receptor (GHSR). In addition, we show that the GHSR:β-arrestin 1 assembly is a dynamic complex where β-arrestin can adopt several orientations. PI(4,5)P2 decreases the dynamics of the complex and shifts the equilibrium between the different arrangements, favoring one of them. Taken together, our results highlight how PI(4,5)P2 plays a true third-player role in the GPCR:β-arrestin interaction, not only by preparing β-arrestin for its further interaction with receptors but also by modulating its orientation once the protein:protein complex is formed.

Indexed as

beta-Arrestin 1beta-ArrestinsPhosphatidylinositol 4,5-DiphosphateReceptors, GhrelinReceptors, G-Protein-CoupledHEK293 CellsHumansLipid BilayersMolecular Dynamics SimulationProtein BindingSignal TransductionSpectrometry, Fluorescencebeta-Arrestin 1beta-ArrestinsLipid BilayersPhosphatidylinositol 4,5-DiphosphateReceptors, GhrelinReceptors, G-Protein-Coupled

Identifiers

PMID40442125
PMCPMC12122939

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.