Evidence map›Paper›PMID 21712381›Full record

ArticleThe Journal of biological chemistry2011

Acireductone dioxygenase 1 (ARD1) is an effector of the heterotrimeric G protein beta subunit in Arabidopsis.

Erin J Friedman, Helen X Wang, Kun Jiang, Iva Perovic, Aditi Deshpande, Thomas C Pochapsky, Brenda R S Temple, Stephanie N Hicks, T Kendall Harden, Alan M Jones

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

26 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
  2. Article
  3. Proteomic profiling ofPhysiology and molecular biology of plants : an international journal of functional plant biology · 2024
    Article
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  5. Article
  6. Review
  7. Article
  8. Overexpression ofFrontiers in plant science · 2019
    Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Review
  15. Article
  16. Review
  17. Article
  18. Heterotrimeric G protein-coupled signaling in plants.Annual review of plant biology · 2014
    Review
  19. Article
  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

10 authors at 2 institutions in 1 country.

Erin J FriedmanDepartment of Biology, University of North Carolina, Chapel Hill, North Carolina 27599, USA.
Helen X Wang
Kun Jiang
Iva Perovic
Aditi Deshpande
Thomas C Pochapsky
Brenda R S Temple
Stephanie N Hicks
T Kendall Harden
Alan M Jones
University of North Carolina at Chapel Hill · USBrandeis 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
STRUCTURE AND DYNAMICS OF METAL-CONTAINING PROTEINSR01GM044191 · NIGMS · BRANDEIS UNIVERSITY · PI POCHAPSKY, THOMAS CHARLES · 1995 to 2012
$3.4M
NCI NIH HHS P30 CA016086NIGMS NIH HHS R01 GM044191NIGMS NIH HHS R01 GM065989NIGMS NIH HHS R01GM065989NIGMS NIH HHS R01-GM44191
6 · The paper itself

Abstract

Heterotrimeric G protein complexes are conserved from plants to mammals, but the complexity of each system varies. Arabidopsis thaliana contains one Gα, one Gβ (AGB1), and at least three Gγ subunits, allowing it to form three versions of the heterotrimer. This plant model is ideal for genetic studies because mammalian systems contain hundreds of unique heterotrimers. The activation of these complexes promotes interactions between both the Gα subunit and the Gβγ dimer with enzymes and scaffolds to propagate signaling to the cytoplasm. However, although effectors of Gα and Gβ are known in mammals, no Gβ effectors were previously known in plants. Toward identifying AGB1 effectors, we genetically screened for dominant mutations that suppress Gβ-null mutant (agb1-2) phenotypes. We found that overexpression of acireductone dioxygenase 1 (ARD1) suppresses the 2-day-old etiolated phenotype of agb1-2. ARD1 is homologous to prokaryotic and eukaryotic ARD proteins; one function of ARDs is to operate in the methionine salvage pathway. We show here that ARD1 is an active metalloenzyme, and AGB1 and ARD1 both control embryonic hypocotyl length by modulating cell division; they also may contribute to the production of ethylene, a product of the methionine salvage pathway. ARD1 physically interacts with AGB1, and ARD enzymatic activity is stimulated by AGB1 in vitro. The binding interface on AGB1 was deduced using a comparative evolutionary approach and tested using recombinant AGB1 mutants. A possible mechanism for AGB1 activation of ARD1 activity was tested using directed mutations in a loop near the substrate-binding site.

Indexed as

ArabidopsisArabidopsis ProteinsBinding SitesCell DivisionDioxygenasesEthylenesGenes, DominantGTP-Binding Protein beta SubunitsHypocotylMethionineMutationProtein BindingProtein Structure, SecondaryRecombinant Proteinsaci-reductone oxidase (CO-forming)AGB1 protein, ArabidopsisArabidopsis ProteinsDioxygenasesethyleneEthylenesGTP-Binding Protein beta SubunitsMethionineRecombinant Proteins

Identifiers

PMID21712381
PMCPMC3191050
OpenAlexW2080094420

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.