Evidence map›Paper›PMID 25601550›Full record

ArticleCurrent biology : CB2015

RGS proteins and septins cooperate to promote chemotropism by regulating polar cap mobility.

Joshua B Kelley, Gauri Dixit, Joshua B Sheetz, Sai Phanindra Venkatapurapu, Timothy C Elston, Henrik G Dohlman

Open access · bronzeAbstract read
In one paragraph

Article in Current biology : CB, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing 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

28 citing papers in PubMed, 48 citations in OpenAlex.

  1. Polarization as a Process: The Potential of Process Ontology for Understanding Cellular Symmetry Breaking.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026
    Review
  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. Article
  8. Article
  9. Orientation of Cell Polarity by Chemical Gradients.Annual review of biophysics · 2022
    Review
  10. Article
  11. Chemotactic movement of a polarity site enables yeast cells to find their mates.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  12. Septins, a cytoskeletal protein family, with emerging role in striated muscle.Journal of muscle research and cell motility · 2021
    Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  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

6 authors at 1 institution in 1 country.

Joshua B KelleyDepartment of Biochemistry and Biophysics, University of North Carolina at Chapel Hill, 120 Mason Farm Road, 3046 Genetic Medicine Building, Campus Box 7260, Chapel Hill, NC 27599, USA; Department of Pharmacology, University of North Carolina at Chapel Hill, 120 Mason Farm Road, 4009 Genetic Medicine Building, Campus Box 7365, Chapel Hill, NC 27599, USA.
Gauri DixitDepartment of Biochemistry and Biophysics, University of North Carolina at Chapel Hill, 120 Mason Farm Road, 3046 Genetic Medicine Building, Campus Box 7260, Chapel Hill, NC 27599, USA.
Joshua B SheetzDepartment of Biochemistry and Biophysics, University of North Carolina at Chapel Hill, 120 Mason Farm Road, 3046 Genetic Medicine Building, Campus Box 7260, Chapel Hill, NC 27599, USA.
Sai Phanindra VenkatapurapuDepartment of Pharmacology, University of North Carolina at Chapel Hill, 120 Mason Farm Road, 4009 Genetic Medicine Building, Campus Box 7365, Chapel Hill, NC 27599, USA; Curriculum in Bioinformatics and Computational Biology, University of North Carolina at Chapel Hill, 120 Mason Farm Road, 4092 Genetic Medicine Building, Campus Box 7365, Chapel Hill, NC 27599, USA.
Timothy C ElstonDepartment of Pharmacology, University of North Carolina at Chapel Hill, 120 Mason Farm Road, 4009 Genetic Medicine Building, Campus Box 7365, Chapel Hill, NC 27599, USA. Electronic address: timothy_elston@med.unc.edu.
Henrik G DohlmanDepartment of Biochemistry and Biophysics, University of North Carolina at Chapel Hill, 120 Mason Farm Road, 3046 Genetic Medicine Building, Campus Box 7260, Chapel Hill, NC 27599, USA; Department of Pharmacology, University of North Carolina at Chapel Hill, 120 Mason Farm Road, 4009 Genetic Medicine Building, Campus Box 7365, Chapel Hill, NC 27599, USA. Electronic address: henrik_dohlman@med.unc.edu.
University of North Carolina at Chapel Hill · US

Funding

Spatiotemporal modeling of signal transduction in yeastR01GM079271 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI ELSTON, TIMOTHY C, ERREDE, BEVERLY · 2006 to 2017
$4.0M
G Protein Signaling at the endosomeR01GM080739 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI DOHLMAN, HENRIK G. · 2007 to 2014
$2.6M
Gradient Tracking and ChemotropismR01GM103870 · NIGMS · DUKE UNIVERSITY · PI ELSTON, TIMOTHY C, LEW, DANIEL J · 2013 to 2016
$1.8M
NIGMS NIH HHS GM079271NIGMS NIH HHS GM080739NIGMS NIH HHS GM103870NIGMS NIH HHS R01 GM079271NIGMS NIH HHS R01 GM080739NIGMS NIH HHS R01 GM103870
6 · The paper itself

Abstract

backgroundSeptins are well known to form a boundary between mother and daughter cells in mitosis, but their role in other morphogenic states is poorly understood.

resultsUsing microfluidics and live-cell microscopy, coupled with new computational methods for image analysis, we investigated septin function during pheromone-dependent chemotropic growth in yeast. We show that septins colocalize with the regulator of G protein signaling (RGS) Sst2, a GTPase-activating protein that dampens pheromone receptor signaling. We show further that the septin structure surrounds the polar cap, ensuring that cell growth is directed toward the source of pheromone. When RGS activity is abrogated, septins are partially disorganized. Under these circumstances, the polar cap travels toward septin structures and away from sites of exocytosis, resulting in a loss of gradient tracking.

conclusionsSeptin organization is dependent on RGS protein activity. When assembled correctly, septins promote turning of the polar cap and proper tracking of a pheromone gradient.

Indexed as

Cell PolarityGTPase-Activating ProteinsImage Processing, Computer-AssistedMicrofluidic Analytical TechniquesModels, BiologicalReceptors, PheromoneRGS ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSeptinsSingle-Cell AnalysisTropismGTPase-Activating ProteinsReceptors, PheromoneRGS ProteinsSaccharomyces cerevisiae ProteinsSeptinsSST2 protein, S cerevisiae

Identifiers

PMID25601550
PMCPMC4318785
OpenAlexW2019816658

What OpenQuestion holds

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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.