Evidence map›Paper›PMID 21685393›Full record

ArticleThe Journal of biological chemistry2011

Pheromone- and RSP5-dependent ubiquitination of the G protein beta subunit Ste4 in yeast.

Ming Zhu, Matthew P Torres, Joshua B Kelley, Henrik G Dohlman, Yuqi Wang

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.7field-weighted citation impact, top 33% 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

11 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
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  4. Article
  5. Regulation of large and small G proteins by ubiquitination.The Journal of biological chemistry · 2019
    Review
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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

5 authors at 2 institutions in 1 country.

Ming ZhuDepartment of Biology, Saint Louis University, St. Louis, Missouri 63103, USA.
Matthew P Torres
Joshua B Kelley
Henrik G Dohlman
Yuqi Wang
University of North Carolina at Chapel Hill · USSaint Louis University · US

Funding

REGULATORS OF G PROTEIN SIGNALING IN YEASTR01GM059167 · NIGMS · YALE UNIVERSITY · PI DOHLMAN, HENRIK G. · 1999 to 2015
$3.7M
G Protein Signaling at the endosomeR01GM080739 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI DOHLMAN, HENRIK G. · 2007 to 2014
$2.6M
Modeling Feedback Regulation of Cell SignalingR01GM073180 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI DOHLMAN, HENRIK G. · 2005 to 2012
$2.6M
Novel Mechanisms Regulating G Protein and MAP Kinase SignalingR15GM093313 · NIGMS · SAINT LOUIS UNIVERSITY · PI WANG, YUQI · 2010 to 2010
$221k
G protein regulation by ubiquitinationK99GM094533 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI TORRES, MATT PHILLIP · 2010 to 2011
$173k
NIGMS NIH HHS K99 GM094533NIGMS NIH HHS K99 GM094533-01NIGMS NIH HHS R01 GM059167NIGMS NIH HHS R01 GM073180NIGMS NIH HHS R01 GM080739NIGMS NIH HHS R15 GM093313NIGMS NIH HHS R15GM093313-01
6 · The paper itself

Abstract

Ste4 is the β subunit of a heterotrimeric G protein that mediates mating responses in Saccharomyces cerevisiae. Here we show that Ste4 undergoes ubiquitination in response to pheromone stimulation. Ubiquitination of Ste4 is dependent on the E3 ligase Rsp5. Disrupting the activity of Rsp5 abolishes ubiquitination of Ste4 in vivo, and recombinant Rsp5 is capable of ubiquitinating Ste4 in vitro. We find also that Lys-340 is a major ubiquitination site on Ste4, as pheromone-induced ubiquitination of the protein is prevented when this residue is mutated to an arginine. Functionally, ubiquitination does not appear to regulate the stability of Ste4, as blocking ubiquitination has no apparent effect on either the abundance or the half-life of the protein. However, when presented with a concentration gradient of pheromone, Ste4(K340R) mutant cells polarize significantly faster than wild-type cells, indicating that ubiquitination limits pheromone-directed polarized growth. Together, these findings reveal a novel stimulus-dependent posttranslational modification of a Gβ subunit, establish Ste4 as a new substrate of the E3 ligase Rsp5, and demonstrate a role for G protein ubiquitination in cell polarization.

Indexed as

Base SequenceDNA PrimersGTP-Binding Protein beta SubunitsMutagenesis, Site-DirectedPheromonesPolymerase Chain ReactionSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitinationDNA PrimersGTP-Binding Protein beta SubunitsPheromonesSaccharomyces cerevisiae ProteinsSte4 protein, S cerevisiae

Identifiers

PMID21685393
PMCPMC3149308
OpenAlexW1968061855

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.