Evidence map›Paper›PMID 25548923›Full record

ArticlePLoS biology2014

Electrochemical regulation of budding yeast polarity.

Armin Haupt, Alexis Campetelli, Daria Bonazzi, Matthieu Piel, Fred Chang, Nicolas Minc

Open access · goldAbstract read
In one paragraph

Article in PLoS biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
4.7field-weighted citation impact, top 6% 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

14 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Electrochemical Response ofBiosensors · 2019
    Article
  5. Article
  6. Review
  7. Electric Pulses Can Influence Galvanotaxis ofBioMed research international · 2018
    Article
  8. Multifunctional scanning ion conductance microscopy.Proceedings. Mathematical, physical, and engineering sciences · 2017
    Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. 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

6 authors at 2 institutions in 2 countries.

Armin HauptInstitut Jacques Monod, UMR7592 CNRS, Paris, France.
Alexis CampetelliInstitut Jacques Monod, UMR7592 CNRS, Paris, France.
Daria BonazziInstitut Jacques Monod, UMR7592 CNRS, Paris, France.
Matthieu PielInstitut Curie, UMR 144 CNRS/IC, Paris, France.
Fred ChangDepartment of Microbiology and Immunology, Columbia University College of Physicians and Surgeons, New York, New York, United States of America.
Nicolas MincInstitut Jacques Monod, UMR7592 CNRS, Paris, France.
Centre National de la Recherche Scientifique · FRColumbia University · US

Funding

ASSEMBLY AND PLACEMENT OF THE CELL DIVISION RINGR01GM056836 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI CHANG, FRED · 1998 to 2018
$7.4M
NIGMS NIH HHS GM056836NIGMS NIH HHS R01 GM056836
6 · The paper itself

Abstract

Cells are naturally surrounded by organized electrical signals in the form of local ion fluxes, membrane potential, and electric fields (EFs) at their surface. Although the contribution of electrochemical elements to cell polarity and migration is beginning to be appreciated, underlying mechanisms are not known. Here we show that an exogenous EF can orient cell polarization in budding yeast (Saccharomyces cerevisiae) cells, directing the growth of mating projections towards sites of hyperpolarized membrane potential, while directing bud emergence in the opposite direction, towards sites of depolarized potential. Using an optogenetic approach, we demonstrate that a local change in membrane potential triggered by light is sufficient to direct cell polarization. Screens for mutants with altered EF responses identify genes involved in transducing electrochemical signals to the polarity machinery. Membrane potential, which is regulated by the potassium transporter Trk1p, is required for polarity orientation during mating and EF response. Membrane potential may regulate membrane charges through negatively charged phosphatidylserines (PSs), which act to position the Cdc42p-based polarity machinery. These studies thus define an electrochemical pathway that directs the orientation of cell polarization.

Indexed as

Cell PolarityElectricityCation Transport Proteinscdc42 GTP-Binding Protein, Saccharomyces cerevisiaeElectrochemistryLipidsMembrane PotentialsModels, BiologicalOptogeneticsPhosphatidylserinesSaccharomyces cerevisiae ProteinsSaccharomycetalesCation Transport Proteinscdc42 GTP-Binding Protein, Saccharomyces cerevisiaeLipidsPhosphatidylserinesSaccharomyces cerevisiae ProteinsTRK1 protein, S cerevisiae

Identifiers

PMID25548923
PMCPMC4280105
OpenAlexW2029401690

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.