Evidence map›Paper›PMID 27235398›Full record

ArticleThe Journal of biological chemistry2016

Direct Modulation of Heterotrimeric G Protein-coupled Signaling by a Receptor Kinase Complex.

Meral Tunc-Ozdemir, Daisuke Urano, Dinesh Kumar Jaiswal, Steven D Clouse, Alan M Jones

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
5.6field-weighted citation impact, top 4% 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

37 citing papers in PubMed, 69 citations in OpenAlex.

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  11. Heterotrimeric G Proteins in Plants: Canonical and Atypical Gα Subunits.International journal of molecular sciences · 2021
    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.

Meral Tunc-OzdemirDepartment of Biology, University of North Carolina, Chapel Hill, North Carolina 27599.
Daisuke UranoDepartment of Biology, University of North Carolina, Chapel Hill, North Carolina 27599.
Dinesh Kumar JaiswalDepartment of Biology, University of North Carolina, Chapel Hill, North Carolina 27599.
Steven D ClouseDepartment of Horticultural Science, North Carolina State University, Raleigh, North Carolina 27695-7609.
Alan M JonesDepartment of Biology, University of North Carolina, Chapel Hill, North Carolina 27599; Department of Pharmacology, University of North Carolina, Chapel Hill, North Carolina 27599. Electronic address: alan_jones@unc.edu.
University of North Carolina at Chapel Hill · USNorth Carolina State University · US

Funding

Virology Research Program (Program 4)P30CA016086 · NCI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI Deborah F. Tate · 1985 to 2026
$201.5M
Novel Mechanisms Regulating the Heterotrimeric G Protein ComplexR01GM065989 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI JONES, ALAN M. · 2002 to 2023
$5.5M
NCI NIH HHS P30 CA016086NIGMS NIH HHS R01 GM065989
6 · The paper itself

Abstract

Plants and some protists have heterotrimeric G protein complexes that activate spontaneously without canonical G protein-coupled receptors (GPCRs). In Arabidopsis, the sole 7-transmembrane regulator of G protein signaling 1 (AtRGS1) modulates the G protein complex by keeping it in the resting state (GDP-bound). However, it remains unknown how a myriad of biological responses is achieved with a single G protein modulator. We propose that in complete contrast to G protein activation in animals, plant leucine-rich repeat receptor-like kinases (LRR RLKs), not GPCRs, provide this discrimination through phosphorylation of AtRGS1 in a ligand-dependent manner. G protein signaling is directly activated by the pathogen-associated molecular pattern flagellin peptide 22 through its LRR RLK, FLS2, and co-receptor BAK1.

Indexed as

ArabidopsisArabidopsis ProteinsFlagellinPeptidesPhosphorylationProtein Serine-Threonine KinasesRGS ProteinsSignal TransductionArabidopsis ProteinsBAK1 protein, ArabidopsisFlagellinPeptidesProtein Serine-Threonine KinasesRGS1 protein, ArabidopsisRGS ProteinsArabidopsis thalianaAtRGS1BAK1flg22FLS2G proteinphosphorylationreceptor-like kinasesreceptor protein serine/threonine kinaseregulator of G protein signaling (RGS)

Identifiers

PMID27235398
PMCPMC4933153
OpenAlexW2398445292

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.