Evidence map›Paper›PMID 16582010›Full record

ArticleThe Plant cell2006

The plastid protein THYLAKOID FORMATION1 and the plasma membrane G-protein GPA1 interact in a novel sugar-signaling mechanism in Arabidopsis.

Jirong Huang, J Philip Taylor, Jin-Gui Chen, Joachim F Uhrig, Danny J Schnell, Tsuyoshi Nakagawa, Kenneth L Korth, Alan M Jones

Open access · bronzeAbstract read
In one paragraph

Article in The Plant cell, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 89 papers.

0numbers the graph read from it
0cells of the map it votes in
89citing papers in PubMed
24.9field-weighted citation impact, top 1% 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

89 citing papers in PubMed, 200 citations in OpenAlex.

  1. Article
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  16. Review
  17. Glucose-RegulatedPlant physiology · 2019
    Article
  18. Chloroplast vesicle transport.Photosynthesis research · 2018
    Review
  19. Characterization of Heterotrimeric G Protein γ4 Subunit in Rice.International journal of molecular sciences · 2018
    Article
  20. Article

29 more citing papers are in PubMed but not listed here.

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

8 authors at 5 institutions in 3 countries.

Jirong HuangDepartment of Biology, University of North Carolina, Chapel Hill, North Carolina 27599, USA.
J Philip Taylor
Jin-Gui Chen
Joachim F Uhrig
Danny J Schnell
Tsuyoshi Nakagawa
Kenneth L Korth
Alan M Jones
University of North Carolina at Chapel Hill · USMax Planck Institute for Plant Breeding Research · DEShimane University · JPUniversity of Arkansas at Fayetteville · USUniversity of Massachusetts Amherst · 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
NIGMS NIH HHS GM65989-01NIGMS NIH HHS R01 GM065989
6 · The paper itself

Abstract

Mutations in genes encoding components of the heterotrimeric G-protein complex were previously shown to confer altered sensitivity to increased levels of D-glucose. This suggests that G-protein coupling may be a novel sugar-signaling mechanism in Arabidopsis thaliana. THYLAKOID FORMATION1 (THF1) is here demonstrated in vivo as a Galpha interaction partner that functions downstream of the plasma membrane-delimited heterotrimeric G-protein (GPA1) in a D-glucose signaling pathway. THF1 is a plastid protein localized to both the outer plastid membrane and the stroma. Contact between root plastidic THF1 and GPA1 at the plasma membrane occurs at sites where the plastid membrane abuts the plasma membrane, as demonstrated by Förster resonance energy transfer (FRET). A probable role for THF1 in sugar signaling is demonstrated by both biochemical and genetic evidence. Root growth in the thf1-1 null mutant is hypersensitive to exogenous D-glucose, and THF1-overexpressing roots are resistant to inhibition of growth rate by high D-glucose. Additionally, THF1 levels are rapidly degraded by D-glucose but not L-glucose. The interaction between THF1 and GPA1 has been confirmed by in vitro and in vivo coimmunoprecipitation, FRET analysis, and genetic epistasis and provides evidence of a sugar-signaling mechanism between plastids and the plasma membrane.

Indexed as

Signal TransductionAmino Acid SequenceArabidopsisArabidopsis ProteinsGlucoseGTP-Binding Protein alpha SubunitsIntracellular MembranesMembrane ProteinsMeristemModels, BiologicalMolecular Sequence DataPlant RootsPlastidsProtein Interaction MappingSequence AlignmentTwo-Hybrid System TechniquesArabidopsis ProteinsGlucoseGPA1 protein, ArabidopsisGTP-Binding Protein alpha SubunitsMembrane ProteinsTHF1 protein, Arabidopsis

Identifiers

PMID16582010
PMCPMC1456876
OpenAlexW2155231024

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.