Evidence map›Paper›PMID 10866688›Full record

ArticleMolecular and cellular biology2000

The C terminus of the Saccharomyces cerevisiae alpha-factor receptor contributes to the formation of preactivation complexes with its cognate G protein.

M Dosil, K A Schandel, E Gupta, D D Jenness, J B Konopka

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2000. 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
1.8field-weighted citation impact, top 15% 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, 64 citations in OpenAlex.

  1. Article
  2. Review
  3. A Paradigm for Peptide Hormone-GPCR Analyses.Molecules (Basel, Switzerland) · 2020
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Fungal mating pheromones: choreographing the dating game.Fungal genetics and biology : FG & B · 2011
    Review
  13. Article
  14. Chemical gradients and chemotropism in yeast.Cold Spring Harbor perspectives in biology · 2009
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  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

5 authors at 2 institutions in 1 country.

M DosilDepartment of Molecular Genetics and Microbiology, State University of New York, Stony Brook, New York 11794-5222, USA.
K A Schandel
E Gupta
D D Jenness
J B Konopka
State University of New York · USUniversity of Massachusetts Chan Medical School · US

Funding

CONTROL OF ALPHA FACTOR RECEPTOR ACTIVITY IN YEAST CELLSR01GM034719 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI JENNESS, DUANE D · 1985 to 2004
$1.6M
ACTIVATION OF G PROTEIN COUPLED RECEPTORSR01GM055107 · NIGMS · STATE UNIVERSITY NEW YORK STONY BROOK · PI KONOPKA, JAMES B. · 1997 to 2004
$1.2M
NIGMS NIH HHS GM34719NIGMS NIH HHS GM55107NIGMS NIH HHS R01 GM034719NIGMS NIH HHS R01 GM055107
6 · The paper itself

Abstract

Binding of the alpha-factor pheromone to its G-protein-coupled receptor (encoded by STE2) activates the mating pathway in MATa yeast cells. To investigate whether specific interactions between the receptor and the G protein occur prior to ligand binding, we analyzed dominant-negative mutant receptors that compete with wild-type receptors for G proteins, and we analyzed the ability of receptors to suppress the constitutive signaling activity of mutant Galpha subunits in an alpha-factor-independent manner. Although the amino acid substitution L236H in the third intracellular loop of the receptor impairs G-protein activation, this substitution had no influence on the ability of the dominant-negative receptors to sequester G proteins or on the ability of receptors to suppress the GPA1-A345T mutant Galpha subunit. In contrast, removal of the cytoplasmic C-terminal domain of the receptor eliminated both of these activities even though the C-terminal domain is unnecessary for G-protein activation. Moreover, the alpha-factor-independent signaling activity of ste2-P258L mutant receptors was inhibited by the coexpression of wild-type receptors but not by coexpression of truncated receptors lacking the C-terminal domain. Deletion analysis suggested that the distal half of the C-terminal domain is critical for sequestration of G proteins. The C-terminal domain was also found to influence the affinity of the receptor for alpha-factor in cells lacking G proteins. These results suggest that the C-terminal cytoplasmic domain of the alpha-factor receptor, in addition to its role in receptor downregulation, promotes the formation of receptor-G-protein preactivation complexes.

Indexed as

GTP-Binding Protein alpha SubunitsSaccharomyces cerevisiae ProteinsTranscription FactorsAllelesAmino Acid SubstitutionCytoplasmGenes, DominantGenes, LethalGTP-Binding Protein alpha Subunits, Gq-G11GTP-Binding ProteinsHeterotrimeric GTP-Binding ProteinsLigandsMutationReceptors, Mating FactorReceptors, PeptideSaccharomyces cerevisiaeGPA1 protein, S cerevisiaeGTP-Binding Protein alpha SubunitsGTP-Binding Protein alpha Subunits, Gq-G11GTP-Binding ProteinsHeterotrimeric GTP-Binding ProteinsLigandsReceptors, Mating FactorReceptors, PeptideSaccharomyces cerevisiae ProteinsTranscription Factors

Identifiers

PMID10866688
PMCPMC85981
OpenAlexW2098539689

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.