Evidence map›Paper›PMID 30559330›Full record

ArticleThe EMBO journal2019

Avidity-driven polarity establishment via multivalent lipid-GTPase module interactions.

Julien Meca, Aurélie Massoni-Laporte, Denis Martinez, Elodie Sartorel, Antoine Loquet, Birgit Habenstein, Derek McCusker

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

23 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
  2. Sortase A-Mediated Farnesylation of Cdc42ACS synthetic biology · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Regulation of yeast polarized exocytosis by phosphoinositide lipids.Cellular and molecular life sciences : CMLS · 2024
    Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Molecular subversion of Cdc42 signalling in cancer.Biochemical Society transactions · 2021
    Review
  12. Review
  13. Lipid flippases in polarized growth.Current genetics · 2021
    Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Review
  19. Review
  20. 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

7 authors at 1 institution in 1 country.

Julien MecaCNRS, UMR 5095, European Institute of Chemistry and Biology, University of Bordeaux, Pessac, France.
Aurélie Massoni-LaporteCNRS, UMR 5095, European Institute of Chemistry and Biology, University of Bordeaux, Pessac, France.
Denis MartinezCNRS, UMR 5248, European Institute of Chemistry and Biology, University of Bordeaux, Pessac, France.
Elodie SartorelCNRS, UMR 5095, European Institute of Chemistry and Biology, University of Bordeaux, Pessac, France.
Antoine LoquetCNRS, UMR 5248, European Institute of Chemistry and Biology, University of Bordeaux, Pessac, France.
Birgit HabensteinCNRS, UMR 5248, European Institute of Chemistry and Biology, University of Bordeaux, Pessac, France.
Derek McCuskerCNRS, UMR 5095, European Institute of Chemistry and Biology, University of Bordeaux, Pessac, France mccusker@iecb.u-bordeaux.fr.ORCID 0000-0003-1455-1711
Centre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

While Rho GTPases are indispensible regulators of cellular polarity, the mechanisms underlying their anisotropic activation at membranes have been elusive. Using the budding yeast Cdc42 GTPase module, which includes a guanine nucleotide exchange factor (GEF) Cdc24 and the scaffold Bem1, we find that avidity generated via multivalent anionic lipid interactions is a critical mechanistic constituent of polarity establishment. We identify basic cluster (BC) motifs in Bem1 that drive the interaction of the scaffold-GEF complex with anionic lipids at the cell pole. This interaction appears to influence lipid acyl chain ordering, thus regulating membrane rigidity and feedback between Cdc42 and the membrane environment. Sequential mutation of the Bem1 BC motifs, PX domain, and the PH domain of Cdc24 lead to a progressive loss of cellular polarity stemming from defective Cdc42 nanoclustering on the plasma membrane and perturbed signaling. Our work demonstrates the importance of avidity via multivalent anionic lipid interactions in the spatial control of GTPase activation.

Indexed as

Cell PolarityAdaptor Proteins, Signal TransducingCell Cycle ProteinsCell MembraneGuanine Nucleotide Exchange FactorsPhosphatidylinositolsPhosphatidylserinesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSignal TransductionAdaptor Proteins, Signal TransducingBEM1 protein, S cerevisiaeCDC24 protein, S cerevisiaeCell Cycle ProteinsGuanine Nucleotide Exchange FactorsPhosphatidylinositolsPhosphatidylserinesSaccharomyces cerevisiae Proteinscell polaritylipidsnanoclusteringRho GTPasesuper‐resolution imaging

Identifiers

PMID30559330
PMCPMC6356062
OpenAlexW2797725092

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.