Evidence map›Paper›PMID 29668348›Full record

ArticleMolecular biology of the cell2018

Phosphatidylserine and GTPase activation control Cdc42 nanoclustering to counter dissipative diffusion.

Elodie Sartorel, Caner Ünlü, Mini Jose, Aurélie Massoni-Laporte, Julien Meca, Jean-Baptiste Sibarita, Derek McCusker

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

22 citing papers in PubMed, 48 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Roles for the canonical polarity machinery in thebioRxiv : the preprint server for biology · 2025
    Article
  5. Article
  6. Article
  7. Membrane Lipids in Epithelial Polarity: Sorting out the PIPs.Frontiers in cell and developmental biology · 2022
    Review
  8. Review
  9. Lipid flippases in polarized growth.Current genetics · 2021
    Review
  10. Review
  11. Review
  12. Review
  13. Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. Review
  19. Review
  20. 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

7 authors at 1 institution in 3 countries.

Elodie SartorelUniversité Bordeaux, CNRS, UMR 5095, European Institute of Chemistry and Biology, Pessac 33607, France.
Caner ÜnlüUniversité Bordeaux, CNRS, UMR 5095, European Institute of Chemistry and Biology, Pessac 33607, France.
Mini JoseUniversité Bordeaux, CNRS, UMR 5095, European Institute of Chemistry and Biology, Pessac 33607, France.
Aurélie Massoni-LaporteUniversité Bordeaux, CNRS, UMR 5095, European Institute of Chemistry and Biology, Pessac 33607, France.
Julien MecaUniversité Bordeaux, CNRS, UMR 5095, European Institute of Chemistry and Biology, Pessac 33607, France.
Jean-Baptiste SibaritaUniversité Bordeaux, Institut Interdisciplinaire de Neurosciences, Bordeaux 33077, France.
Derek McCuskerUniversité Bordeaux, CNRS, UMR 5095, European Institute of Chemistry and Biology, Pessac 33607, France.
Centre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The anisotropic organization of plasma membrane constituents is indicative of mechanisms that drive the membrane away from equilibrium. However, defining these mechanisms is challenging due to the short spatiotemporal scales at which diffusion operates. Here, we use high-density single protein tracking combined with photoactivation localization microscopy (sptPALM) to monitor Cdc42 in budding yeast, a system in which Cdc42 exhibits anisotropic organization. Cdc42 exhibited reduced mobility at the cell pole, where it was organized in nanoclusters. The Cdc42 nanoclusters were larger at the cell pole than those observed elsewhere in the cell. These features were exacerbated in cells expressing Cdc42-GTP, and were dependent on the scaffold Bem1, which contributed to the range of mobility and nanocluster size exhibited by Cdc42. The lipid environment, in particular phosphatidylserine levels, also played a role in regulating Cdc42 nanoclustering. These studies reveal how the mobility of a Rho GTPase is controlled to counter the depletive effects of diffusion, thus stabilizing Cdc42 on the plasma membrane and sustaining cell polarity.

Indexed as

cdc42 GTP-Binding Protein, Saccharomyces cerevisiaeCell MembraneDiffusionMembrane ProteinsNanoparticlesPhosphatidylserinescdc42 GTP-Binding Protein, Saccharomyces cerevisiaeMembrane ProteinsPhosphatidylserines

Identifiers

PMID29668348
PMCPMC5994902
OpenAlexW2801239190

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.