Evidence map›Paper›PMID 30407730›Full record

ArticleProteomics2018

Heterotrimeric G-Protein-Dependent Proteome and Phosphoproteome in Unstimulated Arabidopsis Roots.

Gaoyuan Song, Libuse Brachova, Basil J Nikolau, Alan M Jones, Justin W Walley

Abstract read
In one paragraph

Article in Proteomics, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.5field-weighted citation impact, top 17% 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

13 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Article
  3. ZmPILS6 is an auxin efflux carrier required for maize root morphogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2024
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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.

Gaoyuan SongDepartment of Plant Pathology and Microbiology, Iowa State University, Ames, IA, USA.
Libuse BrachovaDepartment of Biochemistry, Biophysics and Molecular Biology, Iowa State University, Ames, IA, USA.
Basil J NikolauDepartment of Biochemistry, Biophysics and Molecular Biology, Iowa State University, Ames, IA, USA.
Alan M JonesDepartment of Biology and, Department of Pharmacology, University of North Carolina at Chapel Hill, Chapel Hill, NC, USA.
Justin W WalleyDepartment of Plant Pathology and Microbiology, Iowa State University, Ames, IA, USA.ORCID 0000-0001-7553-2237
Iowa State University · USUniversity of North Carolina at Chapel Hill · US

Funding

Novel Mechanisms Regulating the Heterotrimeric G Protein ComplexR01GM065989 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI JONES, ALAN M. · 2002 to 2023
$5.5M
Crosstalk between Brassinosteroid and autophagy pathways in the regulation of plant growth and stress responses: Equipment SupplementR01GM120316 · NIGMS · IOWA STATE UNIVERSITY · PI DIANE C BASSHAM, Justin William Walley · 2017 to 2026
$2.0M
NIGMS NIH HHS 1R01GM120316-01A1NIGMS NIH HHS R01 GM065989NIGMS NIH HHS R01GM065989NIGMS NIH HHS R01 GM120316
6 · The paper itself

Abstract

The G-protein complex is a cytoplasmic on-off molecular switch that is set by plasma membrane receptors that activate upon binding of its cognate extracellular agonist. In animals, the default setting is the "off" resting state, while in plants, the default state is constitutively "on" but repressed by a plasma membrane receptor-like protein. De-repression appears to involve specific phosphorylation of key elements of the G-protein complex and possibly target proteins that are positioned downstream of this complex. To address this possibility, protein abundance and phosphorylation state are quantified in wild type and G-protein deficient Arabidopsis roots in the unstimulated resting state. A total of 3246 phosphorylated and 8141 non-modified protein groups are identified. It has been found that 428 phosphorylation sites decrease and 509 sites increase in abundance in the G-protein quadrupole mutant lacking an operable G-protein-complex. Kinases with known roles in G-protein signaling including MAP KINASE 6 and FERONIA are differentially phosphorylated along with many other proteins now implicated in the control of G-protein signaling. Taken together, these datasets will enable the discovery of novel proteins and biological processes dependent on G-protein signaling.

Indexed as

ArabidopsisArabidopsis ProteinsHeterotrimeric GTP-Binding ProteinsMutationPhosphoproteinsPhosphorylationPlant RootsPlants, Genetically ModifiedProteomeSignal TransductionArabidopsis ProteinsHeterotrimeric GTP-Binding ProteinsPhosphoproteinsProteomeG proteinsTandem Mass Tags

Identifiers

PMID30407730
PMCPMC6298806
OpenAlexW2900310295

What OpenQuestion holds

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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.