Evidence map›Paper›PMID 24003255›Full record

ArticleScience signaling2013

Regulation of yeast G protein signaling by the kinases that activate the AMPK homolog Snf1.

Sarah T Clement, Gauri Dixit, Henrik G Dohlman

Abstract read
In one paragraph

Article in Science signaling, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

25 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Regulation of large and small G proteins by ubiquitination.The Journal of biological chemistry · 2019
    Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Calcineurin, the CaMolecular biology of the cell · 2017
    Article
  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

3 authors at 1 institution in 1 country.

Sarah T ClementDepartment of Biochemistry and Biophysics, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA.
Gauri Dixit
Henrik G Dohlman
University of North Carolina at Chapel Hill · US

Funding

REGULATORS OF G PROTEIN SIGNALING IN YEASTR01GM059167 · NIGMS · YALE UNIVERSITY · PI DOHLMAN, HENRIK G. · 1999 to 2015
$3.7M
NIGMS NIH HHS GM059167NIGMS NIH HHS R01 GM059167
6 · The paper itself

Abstract

Extracellular signals, such as nutrients and hormones, cue intracellular pathways to produce adaptive responses. Often, cells must coordinate their responses to multiple signals to produce an appropriate outcome. We showed that components of a glucose-sensing pathway acted on components of a heterotrimeric guanine nucleotide-binding protein (G protein)-mediated pheromone signaling pathway in the yeast Saccharomyces cerevisiae. We demonstrated that the G protein α subunit Gpa1 was phosphorylated in response to conditions of reduced glucose availability and that this phosphorylation event contributed to reduced pheromone-dependent stimulation of mitogen-activated protein kinases, gene transcription, cell morphogenesis, and mating efficiency. We found that Elm1, Sak1, and Tos3, the kinases that phosphorylate Snf1, the yeast homolog of adenosine monophosphate-activated protein kinase (AMPK), in response to limited glucose availability, also phosphorylated Gpa1 and contributed to the diminished mating response. Reg1, the regulatory subunit of the phosphatase PP1 that acts on Snf1, was likewise required to reverse the phosphorylation of Gpa1 and to maintain the mating response. Thus, the same kinases and phosphatase that regulate Snf1 also regulate Gpa1. More broadly, these results indicate that the pheromone signaling and glucose-sensing pathways communicate directly to coordinate cell behavior.

Indexed as

Enzyme ActivationGTP-Binding Protein alpha Subunits, Gq-G11PheromonesPhosphorylationProtein KinasesProtein Phosphatase 1Protein Serine-Threonine KinasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSignal TransductionELM1 protein, S cerevisiaeGPA1 protein, S cerevisiaeGTP-Binding Protein alpha Subunits, Gq-G11PheromonesPRK1 protein, S cerevisiaeProtein KinasesProtein Phosphatase 1Protein Serine-Threonine KinasesREG1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSNF1-related protein kinasesTOS3 protein, S cerevisiae

Identifiers

PMID24003255
PMCPMC4108480
OpenAlexW2042818464

What OpenQuestion holds

Textmetadata
LicenceTDM
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.