Evidence map›Paper›PMID 36482718›Full record

ArticleBiophysical journal2023

Protein overexpression can induce the elongation of cell membrane nanodomains.

Julie Cornet, Pascal Preira, Laurence Salomé, Frédéric Daumas, Bernard Lagane, Nicolas Destainville, Manoel Manghi, Fabrice Dumas

Open access · greenAbstract read
In one paragraph

Article in Biophysical journal, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.2field-weighted citation impact, top 51% 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

3 citing papers in PubMed, 2 citations in OpenAlex.

  1. Article
  2. Membranes in focus.Biophysical journal · 2023
    Article
  3. EarlyFrontiers in oncology · 2023
    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 5 institutions in 1 country.

Julie CornetLaboratoire de Physique Théorique, Université Toulouse III - Paul Sabatier, CNRS, Toulouse, France.
Pascal PreiraInstitut de Pharmacologie et de Biologie Structurale (IPBS), Université de Toulouse, CNRS, Université Toulouse III - Paul Sabatier (UPS), Toulouse, France.
Laurence SaloméInstitut de Pharmacologie et de Biologie Structurale (IPBS), Université de Toulouse, CNRS, Université Toulouse III - Paul Sabatier (UPS), Toulouse, France.
Frédéric DaumasInstitut de Pharmacologie et de Biologie Structurale (IPBS), Université de Toulouse, CNRS, Université Toulouse III - Paul Sabatier (UPS), Toulouse, France.
Bernard LaganeInfinity, Université de Toulouse III - Paul Sabatier, CNRS, Inserm, Toulouse, France.
Nicolas DestainvilleLaboratoire de Physique Théorique, Université Toulouse III - Paul Sabatier, CNRS, Toulouse, France.
Manoel ManghiLaboratoire de Physique Théorique, Université Toulouse III - Paul Sabatier, CNRS, Toulouse, France. Electronic address: manoel.manghi@univ-tlse3.fr.
Fabrice DumasInstitut de Pharmacologie et de Biologie Structurale (IPBS), Université de Toulouse, CNRS, Université Toulouse III - Paul Sabatier (UPS), Toulouse, France.
Centre National de la Recherche Scientifique · FRInstitut de Pharmacologie et de Biologie Structurale · FRUniversité Fédérale de Toulouse Midi-Pyrénées · FRLaboratoire de Physique Théorique · FRUniversité Toulouse III - Paul Sabatier · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In cell membranes, proteins and lipids are organized into submicrometric nanodomains of varying sizes, shapes, and compositions, performing specific functions. Despite their biological importance, the detailed morphology of these nanodomains remains unknown. Not only can they hardly be observed by conventional microscopy due to their small size, but there is no full consensus on the theoretical models to describe their structuring and their shapes. Here, we use a combination of analytical calculations and Monte Carlo simulations based upon a model coupling membrane composition and shape to show that increasing protein concentration leads to an elongation of membrane nanodomains. The results are corroborated by single-particle tracking measurements on HIV receptors, whose level of expression in the membrane of specifically designed living cells can be tuned. These findings highlight that protein abundance can modulate nanodomain shape and potentially their biological function. Beyond biomembranes, this mesopatterning mechanism is of relevance in several soft-matter systems because it relies on generic physical arguments.

Indexed as

MicroscopySingle Molecule ImagingCell MembraneMembrane Microdomains

Identifiers

PMID36482718
PMCPMC10257090
OpenAlexW4310947836

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.