Evidence map›Paper›PMID 34158397›Full record

ArticleScience signaling2021

Combinatorial phosphorylation modulates the structure and function of the G protein γ subunit in yeast.

Zahra Nassiri Toosi, Xinya Su, Ruth Austin, Shilpa Choudhury, Wei Li, Yui Tik Pang, James C Gumbart, Matthew P Torres

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Science signaling, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.3field-weighted citation impact, top 44% 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

2 citing papers in PubMed, 6 citations in OpenAlex.

  1. Article
  2. Review
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

8 authors at 1 institution in 1 country.

Zahra Nassiri ToosiSchool of Biological Sciences, Georgia Institute of Technology, Atlanta, GA 30332, USA.ORCID 0000-0002-8207-151X
Xinya SuSchool of Biological Sciences, Georgia Institute of Technology, Atlanta, GA 30332, USA.ORCID 0000-0001-8437-3573
Ruth AustinSchool of Biological Sciences, Georgia Institute of Technology, Atlanta, GA 30332, USA.ORCID 0000-0002-8050-4094
Shilpa ChoudhurySchool of Biological Sciences, Georgia Institute of Technology, Atlanta, GA 30332, USA.
Wei LiSchool of Biological Sciences, Georgia Institute of Technology, Atlanta, GA 30332, USA.ORCID 0000-0002-9613-6804
Yui Tik PangSchool of Physics, Georgia Institute of Technology, Atlanta, GA 30332, USA.ORCID 0000-0003-4843-4468
James C GumbartSchool of Physics, Georgia Institute of Technology, Atlanta, GA 30332, USA.ORCID 0000-0002-1510-7842
Matthew P TorresSchool of Biological Sciences, Georgia Institute of Technology, Atlanta, GA 30332, USA. mtorres35@gatech.edu.ORCID 0000-0001-7296-4536
Georgia Institute of Technology · US

Funding

Dynamic characterization of outer-membrane-protein biogenesis by the BAM and TAM complexesR01GM123169 · NIGMS · GEORGIA INSTITUTE OF TECHNOLOGY · PI GUMBART, JAMES C. · 2017 to 2021
$1.4M
G gamma N-terminal tails as regulators of G protein signalingR01GM117400 · NIGMS · GEORGIA INSTITUTE OF TECHNOLOGY · PI TORRES, MATT PHILLIP · 2016 to 2019
$1.2M
NIGMS NIH HHS R01 GM117400NIGMS NIH HHS R01 GM123169
6 · The paper itself

Abstract

Intrinsically disordered regions (IDRs) in proteins are often targets of combinatorial posttranslational modifications, which serve to regulate protein structure and function. Emerging evidence suggests that the N-terminal tails of G protein γ subunits, which are essential components of heterotrimeric G proteins, are intrinsically disordered, phosphorylation-dependent determinants of G protein signaling. Here, we found that the yeast Gγ subunit Ste18 underwent combinatorial, multisite phosphorylation events within its N-terminal IDR. G protein-coupled receptor (GPCR) activation and osmotic stress induced phosphorylation at Ser

Indexed as

GTP-Binding Protein gamma SubunitsHeterotrimeric GTP-Binding ProteinsSaccharomyces cerevisiae ProteinsPhosphorylationSaccharomyces cerevisiaeGTP-Binding Protein gamma SubunitsHeterotrimeric GTP-Binding ProteinsSaccharomyces cerevisiae ProteinsSTE18 protein, S cerevisiae

Identifiers

PMID34158397
PMCPMC8427513
OpenAlexW3176495418

What Socratic 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 Socratic graph.