Evidence map›Paper›PMID 16467474›Full record

ArticleEukaryotic cell2006

Genome-scale analysis reveals Sst2 as the principal regulator of mating pheromone signaling in the yeast Saccharomyces cerevisiae.

Scott A Chasse, Paul Flanary, Stephen C Parnell, Nan Hao, Jiyoung Y Cha, David P Siderovski, Henrik G Dohlman

Open access · diamondAbstract read
In one paragraph

Article in Eukaryotic cell, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

39 citing papers in PubMed, 69 citations in OpenAlex.

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  11. Mitotic and pheromone-specific intrinsic polarization cues interfere with gradient sensing inProceedings of the National Academy of Sciences of the United States of America · 2020
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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

7 authors at 2 institutions in 2 countries.

Scott A ChasseDepartment of Biochemistry and Biophysics, University of North Carolina, Chapel Hill, NC 27599-7260, USA.
Paul Flanary
Stephen C Parnell
Nan Hao
Jiyoung Y Cha
David P Siderovski
Henrik G Dohlman
Institute of Molecular Biology and Biophysics · RUUniversity of North Carolina at Chapel Hill · US

Funding

Structures of Novel R7 and R12 RGS Protein DomainsP01GM065533 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI HARDEN, T KENDALL · 2002 to 2006
$6.0M
NIGMS NIH HHS P01 GM065533NIGMS NIH HHS P01-GM65533
6 · The paper itself

Abstract

A common property of G protein-coupled receptors is that they become less responsive with prolonged stimulation. Regulators of G protein signaling (RGS proteins) are well known to accelerate G protein GTPase activity and do so by stabilizing the transition state conformation of the G protein alpha subunit. In the yeast Saccharomyces cerevisiae there are four RGS-homologous proteins (Sst2, Rgs2, Rax1, and Mdm1) and two Galpha proteins (Gpa1 and Gpa2). We show that Sst2 is the only RGS protein that binds selectively to the transition state conformation of Gpa1. The other RGS proteins also bind Gpa1 and modulate pheromone signaling, but to a lesser extent and in a manner clearly distinct from Sst2. To identify other candidate pathway regulators, we compared pheromone responses in 4,349 gene deletion mutants representing nearly all nonessential genes in yeast. A number of mutants produced an increase (sst2, bar1, asc1, and ygl024w) or decrease (cla4) in pheromone sensitivity or resulted in pheromone-independent signaling (sst2, pbs2, gas1, and ygl024w). These findings suggest that Sst2 is the principal regulator of Gpa1-mediated signaling in vivo but that other proteins also contribute in distinct ways to pathway regulation.

Indexed as

Signal TransductionAmino Acid SequenceGene DeletionGene Expression Regulation, FungalGenome, FungalGenomicsGTPase-Activating ProteinsGTP-Binding Protein alpha SubunitsGTP-Binding Protein alpha Subunits, Gq-G11Mating FactorMitogen-Activated Protein KinasesMolecular Sequence DataPeptidesPheromonesPlasmidsProtein BindingGPA1 protein, S cerevisiaeGTPase-Activating ProteinsGTP-Binding Protein alpha SubunitsGTP-Binding Protein alpha Subunits, Gq-G11Mating FactorMitogen-Activated Protein KinasesPeptidesPheromonesRGS ProteinsSaccharomyces cerevisiae ProteinsSST2 protein, S cerevisiae

Identifiers

PMID16467474
PMCPMC1405904
OpenAlexW2162582432

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.