Evidence map›Paper›PMID 26498905›Full record

ArticleThe Plant cell2015

Phosphorylation-Dependent Regulation of G-Protein Cycle during Nodule Formation in Soybean.

Swarup Roy Choudhury, Sona Pandey

Erratum issuedAbstract read
In one paragraph

Article in The Plant cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
–field-weighted citation impact
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

32 citing papers in PubMed.

  1. Article
  2. The coupling effect ofSynthetic and systems biotechnology · 2026
    Article
  3. Article
  4. Review
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  6. Article
  7. Review
  8. Review
  9. Review
  10. Heterotrimeric G Proteins in Plants: Canonical and Atypical Gα Subunits.International journal of molecular sciences · 2021
    Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Review
  18. Article
  19. Article
  20. Early signalling mechanisms underlying receptor kinase-mediated immunity in plants.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2019
    Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors.

Swarup Roy ChoudhuryDonald Danforth Plant Science Center, St. Louis, Missouri 63132.ORCID http://orcid.org/0000-0002-6738-3574
Sona PandeyDonald Danforth Plant Science Center, St. Louis, Missouri 63132 spandey@danforthcenter.org.ORCID http://orcid.org/0000-0002-5570-3120

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Signaling pathways mediated by heterotrimeric G-protein complexes comprising Gα, Gβ, and Gγ subunits and their regulatory RGS (Regulator of G-protein Signaling) protein are conserved in all eukaryotes. We have shown that the specific Gβ and Gγ proteins of a soybean (Glycine max) heterotrimeric G-protein complex are involved in regulation of nodulation. We now demonstrate the role of Nod factor receptor 1 (NFR1)-mediated phosphorylation in regulation of the G-protein cycle during nodulation in soybean. We also show that during nodulation, the G-protein cycle is regulated by the activity of RGS proteins. Lower or higher expression of RGS proteins results in fewer or more nodules, respectively. NFR1 interacts with RGS proteins and phosphorylates them. Analysis of phosphorylated RGS protein identifies specific amino acids that, when phosphorylated, result in significantly higher GTPase accelerating activity. These data point to phosphorylation-based regulation of G-protein signaling during nodule development. We propose that active NFR1 receptors phosphorylate and activate RGS proteins, which help maintain the Gα proteins in their inactive, trimeric conformation, resulting in successful nodule development. Alternatively, RGS proteins might also have a direct role in regulating nodulation because overexpression of their phospho-mimic version leads to partial restoration of nodule formation in nod49 mutants.

Indexed as

Gene Expression Regulation, PlantGenes, PlantGlycine maxGTP-Binding ProteinsModels, BiologicalPhosphorylationPlant ProteinsPlant Root NodulationPlants, Genetically ModifiedProtein BindingReceptors, Cell SurfaceRGS ProteinsRoot Nodules, PlantGTP-Binding ProteinsPlant ProteinsReceptors, Cell SurfaceRGS Proteins

Identifiers

PMID26498905
PMCPMC4682299

What OpenQuestion holds

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Registered trials

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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.