Evidence map›Paper›PMID 31693794›Full record

ArticleProteomics2019

Receptor-Like Kinase Phosphorylation of Arabidopsis Heterotrimeric G-Protein Gα -Subunit AtGPA1.

Haiyan Jia, Gaoyuan Song, Emily G Werth, Justin W Walley, Leslie M Hicks, Alan M Jones

Open access · greenAbstract read
In one paragraph

Article in Proteomics, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.6field-weighted citation impact, top 32% 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

10 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Journal of genetics · 2025
    Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. A Sugarcane G-Protein-Coupled Receptor,Frontiers in plant science · 2021
    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

6 authors at 2 institutions in 1 country.

Haiyan JiaDepartment of Biology, University of North Carolina at Chapel Hill, Chapel Hill, NC, 27599, USA.
Gaoyuan SongDepartment of Plant Pathology and Microbiology, Iowa State University, Ames, IA, 50011, USA.
Emily G WerthDepartment of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, NC, 27599, USA.
Justin W WalleyDepartment of Plant Pathology and Microbiology, Iowa State University, Ames, IA, 50011, USA.
Leslie M HicksDepartment of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, NC, 27599, USA.
Alan M JonesDepartment of Biology, University of North Carolina at Chapel Hill, Chapel Hill, NC, 27599, USA.
University of North Carolina at Chapel Hill · USIowa State University · 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 R01 GM065989NIGMS NIH HHS R01GM065989NIGMS NIH HHS R01 GM120316NIGMS NIH HHS R01GM120316
6 · The paper itself

Abstract

As molecular on-off switches, heterotrimeric G protein complexes, comprised of a Gα subunit and an obligate Gβγ dimer, transmit extracellular signals received by G protein-coupled receptors (GPCRs) to cytoplasmic targets that respond to biotic and abiotic stimuli. Signal transduction is modulated by phosphorylation of GPCRs and G protein complexes. In Arabidopsis thaliana, the Gα subunit AtGPA1 is phosphorylated by the receptor-like kinase (RLK) BRI1-associated Kinase 1 (BAK1), but the extent that other RLKs phosphorylates AtGPA1 is unknown. Twenty-two trans-phosphorylation sites on AtGPA1 are mapped by 12 RLKs hypothesized to act in the Arabidopsis G protein signaling pathway. Cis-phosphorylation sites are also identified on these RLKs, some newly shown to be dual specific kinases. Multiple sites are present in the core AtGPA1 functional units, including pSer52 and/or pThr53 of the conserved P-loop that directly binds nucleotide/phosphate, pThr164, and pSer175 from αE helix in the intramolecular domain interface for nucleotide exchange and GTP hydrolysis, and pThr193 and/or pThr194 in Switch I (SwI) that coordinates nucleotide exchange and protein partner binding. Several AtGPA1 S/T phosphorylation sites are potentially nucleotide-dependent phosphorylation patterns, such as Ser52/Thr53 in the P-loop and Thr193 and/or Thr194 in SwI.

Indexed as

Gene Expression Regulation, PlantArabidopsisArabidopsis ProteinsGTP-Binding Protein alpha SubunitsPhosphorylationProtein BindingProtein Serine-Threonine KinasesSignal TransductionArabidopsis ProteinsGPA1 protein, ArabidopsisGTP-Binding Protein alpha SubunitsProtein Serine-Threonine KinasesArabidopsisArabidopsis thaliana GPA1 (AtGPA1)G protein alpha subunitheterotrimeric G proteinphosphorylationreceptor-like kinasesReceptor Like Kinases (RLKs)

Identifiers

PMID31693794
PMCPMC7014827
OpenAlexW2987871642

What OpenQuestion 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 OpenQuestion graph.