Evidence map›Paper›PMID 25430066›Full record

ArticleThe Plant journal : for cell and molecular biology2015

Evidence for an unusual transmembrane configuration of AGG3, a class C Gγ subunit of Arabidopsis.

Susanne Wolfenstetter, David Chakravorty, Ryan Kula, Daisuke Urano, Yuri Trusov, Michael B Sheahan, David W McCurdy, Sarah M Assmann, Alan M Jones, José R Botella

Open access · greenAbstract read
In one paragraph

Article in The Plant journal : for cell and molecular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

24 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Agronomic potential of plant-specific Gγ proteins.Physiology and molecular biology of plants : an international journal of functional plant biology · 2024
    Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
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  15. Review
  16. Article
  17. Article
  18. Variations inBreeding science · 2016
    Article
  19. 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

10 authors at 5 institutions in 2 countries.

Susanne WolfenstetterDepartment of Biology, University of North Carolina, Chapel Hill, NC, 27599, USA.
David Chakravorty
Ryan Kula
Daisuke Urano
Yuri Trusov
Michael B Sheahan
David W McCurdy
Sarah M Assmann
Alan M Jones
José R Botella
University of North Carolina at Chapel Hill · USPennsylvania State University · USUniversity of Newcastle Australia · AUAgriculture and Food · AUUniversity of Queensland · AU

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 R01 GM065989NIGMS NIH HHS R01GM065989
6 · The paper itself

Abstract

Heterotrimeric G proteins are crucial for the perception of external signals and subsequent signal transduction in animal and plant cells. In both model systems, the complex comprises one Gα, one Gβ, and one Gγ subunit. However, in addition to the canonical Gγ subunits (class A), plants also possess two unusual, plant-specific classes of Gγ subunits (classes B and C) that have not yet been found in animals. These include Gγ subunits lacking the C-terminal CaaX motif (class B), which is important for membrane anchoring of the protein; the presence of such subunits gives rise to a flexible sub-population of Gβ/γ heterodimers that are not necessarily restricted to the plasma membrane. Plants also contain class C Gγ subunits, which are twice the size of canonical Gγ subunits, with a predicted transmembrane domain and a large cysteine-rich extracellular C-terminus. However, neither the presence of the transmembrane domain nor the membrane topology have been unequivocally demonstrated. Here, we provide compelling evidence that AGG3, a class C Gγ subunit of Arabidopsis, contains a functional transmembrane domain, which is sufficient but not essential for plasma membrane localization, and that the cysteine-rich C-terminus is extracellular.

Indexed as

ArabidopsisArabidopsis ProteinsCell MembraneGTP-Binding Protein alpha SubunitsGTP-Binding Protein beta SubunitsGTP-Binding Protein gamma SubunitsModels, MolecularPhylogenyProtein Structure, TertiarySequence Analysis, ProteinAGB1 protein, ArabidopsisAGG3 protein, ArabidopsisArabidopsis ProteinsGPA1 protein, ArabidopsisGTP-Binding Protein alpha SubunitsGTP-Binding Protein beta SubunitsGTP-Binding Protein gamma SubunitsArabidopsis Gγ subunit 3, AGG3Arabidopsis thalianaheterotrimeric G proteinmembrane topologytype II membrane protein

Identifiers

PMID25430066
PMCPMC4334566
OpenAlexW2112734209

What OpenQuestion holds

Textmetadata
LicenceTDM
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.