Evidence map›Paper›PMID 34445169›Full record

ArticleInternational journal of molecular sciences2021

CD82 and Gangliosides Tune CD81 Membrane Behavior.

Laurent Fernandez, Morgane Malrieu, Christine Bénistant, Patrice Dosset, Eric Rubinstein, Elena Odintsova, Fedor Berditchevski, Pierre-Emmanuel Milhiet

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.2field-weighted citation impact, top 23% 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

6 citing papers in PubMed, 11 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Review
  5. Renal CD81 interacts with sodium potassium 2 chloride cotransporter and sodium chloride cotransporter in rats with lipopolysaccharide-induced preeclampsia.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2023
    Article
  6. Membrane Proteins: Structure, Function and Motion.International journal of molecular sciences · 2022
    Article
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

8 authors at 3 institutions in 2 countries.

Laurent FernandezCentre de Biologie Structurale (CBS), INSERM (National Institute of Health and Medical Research), CNRS (Centre National de la Recherche Scientifique), Université de Montpellier, 34090 Montpellier, France.
Morgane MalrieuCentre de Biologie Structurale (CBS), INSERM (National Institute of Health and Medical Research), CNRS (Centre National de la Recherche Scientifique), Université de Montpellier, 34090 Montpellier, France.
Christine BénistantCentre de Biologie Structurale (CBS), INSERM (National Institute of Health and Medical Research), CNRS (Centre National de la Recherche Scientifique), Université de Montpellier, 34090 Montpellier, France.
Patrice DossetCentre de Biologie Structurale (CBS), INSERM (National Institute of Health and Medical Research), CNRS (Centre National de la Recherche Scientifique), Université de Montpellier, 34090 Montpellier, France.
Eric RubinsteinINSERM (National Institute of Health and Medical Research), U602, 94807 Villejuif, France.ORCID 0000-0001-7623-9665
Elena OdintsovaInstitute of Cancer and Genomic Sciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, UK.
Fedor BerditchevskiInstitute of Cancer and Genomic Sciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, UK.
Pierre-Emmanuel MilhietCentre de Biologie Structurale (CBS), INSERM (National Institute of Health and Medical Research), CNRS (Centre National de la Recherche Scientifique), Université de Montpellier, 34090 Montpellier, France.ORCID 0000-0002-0410-5956
Centre National de la Recherche Scientifique · FRUniversity of Birmingham · GBInserm · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tetraspanins are a family of transmembrane proteins that form a network of protein-protein interactions within the plasma membrane. Within this network, tetraspanin are thought to control the lateral segregation of their partners at the plasma membrane through mechanisms involving specific lipids. Here, we used a single molecule tracking approach to study the membrane behavior of tetraspanins in mammary epithelial cells and demonstrate that despite a common overall behavior, each tetraspanin (CD9, CD81 and CD82) has a specific signature in terms of dynamics. Furthermore, we demonstrated that tetraspanin dynamics on the cell surface are dependent on gangliosides. More specifically, we found that CD82 expression increases the dynamics of CD81 and alters its localization at the plasma membrane, this has no effect on the behavior of CD9. Our results provide new information on the ability of CD82 and gangliosides to differentially modulate the dynamics and organization of tetraspanins at the plasma membrane and highlight that its lipid and protein composition is involved in the dynamical architecture of the tetraspanin web. We predict that CD82 may act as a regulator of the lateral segregation of specific tetraspanins at the plasma membrane while gangliosides could play a crucial role in establishing tetraspanin-enriched areas.

Indexed as

Cell MembraneCells, CulturedEpithelial CellsGangliosidesHumansKangai-1 ProteinMembrane MicrodomainsTetraspanin 28CD81 protein, humanCD82 protein, humanGangliosidesKangai-1 ProteinTetraspanin 28CD81CD82fluorescence microscopygangliosidesmembrane diffusionmicrodomainsingle-molecule trackingtetraspanins

Identifiers

PMID34445169
PMCPMC8395132
OpenAlexW3189829005

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.