Evidence map›Paper›PMID 26157115›Full record

ArticlePlant physiology2015

Extra-Large G Proteins Expand the Repertoire of Subunits in Arabidopsis Heterotrimeric G Protein Signaling.

David Chakravorty, Timothy E Gookin, Matthew J Milner, Yunqing Yu, Sarah M Assmann

Open access · greenAbstract read
In one paragraph

Article in Plant physiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
5.4field-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

57 citing papers in PubMed, 116 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Journal of genetics · 2025
    Article
  5. Article
  6. Review
  7. Article
  8. Overexpression ofPlants (Basel, Switzerland) · 2024
    Article
  9. Article
  10. Article
  11. An atypical heterotrimeric Gα and its interactome suggest an extra-large role in overcoming abiotic and biotic stress.Physiology and molecular biology of plants : an international journal of functional plant biology · 2023
    Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Review
  18. Article
  19. Heterotrimeric G Proteins in Plants: Canonical and Atypical Gα Subunits.International journal of molecular sciences · 2021
    Review
  20. 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

5 authors at 1 institution in 1 country.

David ChakravortyBiology Department, Pennsylvania State University, University Park, Pennsylvania 16802.ORCID http://orcid.org/0000-0002-6591-4853
Timothy E GookinBiology Department, Pennsylvania State University, University Park, Pennsylvania 16802.ORCID http://orcid.org/0000-0002-0994-0790
Matthew J MilnerBiology Department, Pennsylvania State University, University Park, Pennsylvania 16802.ORCID http://orcid.org/0000-0001-9184-7423
Yunqing YuBiology Department, Pennsylvania State University, University Park, Pennsylvania 16802.
Sarah M AssmannBiology Department, Pennsylvania State University, University Park, Pennsylvania 16802 sma3@psu.edu.ORCID http://orcid.org/0000-0003-4541-1594
Pennsylvania State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Heterotrimeric G proteins, consisting of Gα, Gβ, and Gγ subunits, are a conserved signal transduction mechanism in eukaryotes. However, G protein subunit numbers in diploid plant genomes are greatly reduced as compared with animals and do not correlate with the diversity of functions and phenotypes in which heterotrimeric G proteins have been implicated. In addition to GPA1, the sole canonical Arabidopsis (Arabidopsis thaliana) Gα subunit, Arabidopsis has three related proteins: the extra-large GTP-binding proteins XLG1, XLG2, and XLG3. We demonstrate that the XLGs can bind Gβγ dimers (AGB1 plus a Gγ subunit: AGG1, AGG2, or AGG3) with differing specificity in yeast (Saccharomyces cerevisiae) three-hybrid assays. Our in silico structural analysis shows that XLG3 aligns closely to the crystal structure of GPA1, and XLG3 also competes with GPA1 for Gβγ binding in yeast. We observed interaction of the XLGs with all three Gβγ dimers at the plasma membrane in planta by bimolecular fluorescence complementation. Bioinformatic and localization studies identified and confirmed nuclear localization signals in XLG2 and XLG3 and a nuclear export signal in XLG3, which may facilitate intracellular shuttling. We found that tunicamycin, salt, and glucose hypersensitivity and increased stomatal density are agb1-specific phenotypes that are not observed in gpa1 mutants but are recapitulated in xlg mutants. Thus, XLG-Gβγ heterotrimers provide additional signaling modalities for tuning plant G protein responses and increase the repertoire of G protein heterotrimer combinations from three to 12. The potential for signal partitioning and competition between the XLGs and GPA1 is a new paradigm for plant-specific cell signaling.

Indexed as

Signal TransductionAmino Acid SequenceArabidopsisArabidopsis ProteinsCell MembraneComputer SimulationGTP-Binding ProteinsHeterotrimeric GTP-Binding ProteinsMolecular Sequence DataMutationNicotianaNuclear Localization SignalsPhenotypeProtein BindingProtein SubunitsSubcellular FractionsArabidopsis ProteinsGTP-Binding ProteinsHeterotrimeric GTP-Binding ProteinsNuclear Localization SignalsProtein SubunitsTunicamycinXLG1 protein, ArabidopsisXLG2 protein, ArabidopsisXLG3 protein, Arabidopsis

Identifiers

PMID26157115
PMCPMC4577375
OpenAlexW2140339883

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.