Evidence map›Paper›PMID 20075078›Full record

ArticleThe Journal of biological chemistry2010

G proteins in reverse mode: receptor-mediated GTP release inhibits G protein and effector function.

Leif G Hommers, Christoph Klenk, Christian Dees, Moritz Bünemann

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

10 citing papers in PubMed, 18 citations in OpenAlex.

  1. Innovative Approach Reveals How Receptors Control G Protein State Equilibria.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Heterotrimeric GThe Journal of biological chemistry · 2020
    Review
  6. Review
  7. Lifetime of muscarinic receptor-G-protein complexes determines coupling efficiency and G-protein subtype selectivity.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  8. Article
  9. Review
  10. 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

4 authors at 1 institution in 1 country.

Leif G HommersInstitute of Pharmacology & Toxicology, University of Würzburg, 97078 Würzburg, Germany.
Christoph Klenk
Christian Dees
Moritz Bünemann
University of Würzburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Active G protein-coupled receptors activate heterotrimeric Galphabetagamma proteins by catalyzing the exchange of GDP by GTP at the Galpha subunit. A paradoxical attenuation of G protein-activated inwardly rectifying potassium channels (GIRK) upon stimulation of native cells with high concentrations of agonist is known. However, a deactivation of activated G proteins by active receptors has not been experimentally studied in intact cells. We monitored GIRK currents and G(o) protein activation by means of fluorescence resonance energy transfer (FRET) in parallel. The results suggested that GIRK currents were paradoxically attenuated due to an inactivation of G(o) proteins by active alpha(2A)-adrenergic receptors. To study the mechanisms, G protein activation and receptor-G protein interactions were analyzed as a function of nucleotide type and nucleotide concentrations by means of FRET, while controlling intracellular nucleotides upon permeabilization of the cell membrane. Results suggested a receptor-catalyzed dissociation of GTP from activated heterotrimeric Galphabetagamma. Consequently, nucleotide-free G proteins were sequestrated in heterotrimeric conformation at the active receptor, thus attenuating downstream signaling in an agonist-dependent manner.

Indexed as

Cells, CulturedFluorescence Resonance Energy TransferG Protein-Coupled Inwardly-Rectifying Potassium ChannelsGTP-Binding Protein alpha SubunitsGTP-Binding Protein beta SubunitsGTP-Binding Protein gamma SubunitsGTP-Binding ProteinsGuanosine 5'-O-(3-Thiotriphosphate)Guanosine TriphosphateHeterotrimeric GTP-Binding ProteinsHumansKidneyPatch-Clamp TechniquesReceptors, Adrenergic, alpha-2Receptors, G-Protein-CoupledSignal TransductionADRA2A protein, humanG Protein-Coupled Inwardly-Rectifying Potassium ChannelsGTP-Binding Protein alpha SubunitsGTP-Binding Protein beta SubunitsGTP-Binding Protein gamma SubunitsGTP-Binding ProteinsGuanosine 5'-O-(3-Thiotriphosphate)Guanosine TriphosphateHeterotrimeric GTP-Binding ProteinsReceptors, Adrenergic, alpha-2Receptors, G-Protein-Coupled

Identifiers

PMID20075078
PMCPMC2832974
OpenAlexW2009828979

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.