Evidence map›Paper›PMID 10725354›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2000

Signal transduction by a nondissociable heterotrimeric yeast G protein.

S Klein, H Reuveni, A Levitzki

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

36 citing papers in PubMed, 90 citations in OpenAlex.

  1. Review
  2. Article
  3. Heterotrimeric G Proteins in Plants: Canonical and Atypical Gα Subunits.International journal of molecular sciences · 2021
    Review
  4. Article
  5. Article
  6. Review
  7. Review
  8. Monitoring ligand-dependent assembly of receptor ternary complexes in live cells by BRETFect.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  9. Review
  10. Frontiers in plant science · 2017
    Article
  11. Single-cell dynamics and variability of MAPK activity in a yeast differentiation pathway.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  12. Review
  13. The GPCR heterotetramer: challenging classical pharmacology.Trends in pharmacological sciences · 2015
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. 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 2 institutions in 2 countries.

S KleinDepartment of Biological Chemistry, Alexander Silverman Institute of Life Sciences, The Hebrew University of Jerusalem, Givat Ram, Jerusalem 91904, Israel.
H Reuveni
A Levitzki
Hebrew University of Jerusalem · ILStanford University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Many signal transduction pathways involve heterotrimeric G proteins. The accepted model for activation of heterotrimeric G proteins states that the protein dissociates to the free G(alpha) (GTP)-bound subunit and free G(betagamma) dimer. On GTP hydrolysis, G(alpha) (GDP) then reassociates with G(betagamma) [Gilman, A. G. (1987) Annu. Rev. Biochem. 56, 615-649]. We reexamined this hypothesis, by using the mating G protein of the yeast Saccharomyces cerevisiae encoded by the genes GPA1, STE4, and STE18. In the absence of mating pheromone, the G(alpha) (Gpa1) subunit represses the mating pathway. On activation by binding of pheromone to a serpentine receptor, the G(betagamma) (Ste4, Ste18) dimer transmits the signal to a mitogen-activated protein kinase cascade, leading to gene activation, arrest in the G(1) stage of the cell cycle, production of shmoos (mating projections), and cell fusion. We found that a Ste4-Gpa1 fusion protein transmitted the pheromone signal and activated the mating pathway as effectively as when Ste4 (G(beta)) and Gpa1 (G(alpha)) were coexpressed as separate proteins. Hence, dissociation of this G protein is not required for its activation. Rather, a conformational change in the heterotrimeric complex is likely to be involved in signal transduction.

Indexed as

GTP-Binding Protein alpha SubunitsGTP-Binding Protein beta SubunitsSaccharomyces cerevisiae ProteinsSignal TransductionBlotting, WesternGTP-Binding Protein alpha Subunits, Gq-G11Heterotrimeric GTP-Binding ProteinsLipoproteinsPheromonesRecombinant Fusion ProteinsSaccharomyces cerevisiaeGPA1 protein, S cerevisiaeGTP-Binding Protein alpha SubunitsGTP-Binding Protein alpha Subunits, Gq-G11GTP-Binding Protein beta SubunitsHeterotrimeric GTP-Binding ProteinsLipoproteinsMFA2 protein, S cerevisiaePheromonesRecombinant Fusion ProteinsSaccharomyces cerevisiae ProteinsSte4 protein, S cerevisiae

Identifiers

PMID10725354
PMCPMC16219
OpenAlexW2117047073

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.