Evidence map›Paper›PMID 10485876›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1999

Crosstalk between Galpha(i)- and Galpha(q)-coupled receptors is mediated by Gbetagamma exchange.

U Quitterer, M J Lohse

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

30 citing papers in PubMed, 82 citations in OpenAlex.

  1. A molecular mechanism to diversify CaNature communications · 2024
    Article
  2. Review
  3. Molecular regulation of PLCβ signaling.Methods in enzymology · 2023
    Review
  4. Functional coupling of MEuropean archives of psychiatry and clinical neuroscience · 2020
    Article
  5. Article
  6. Receptor-specific crosstalk between prostanoid E receptor 3 and bombesin receptor subtype 3.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2018
    Article
  7. βNature chemical biology · 2017
    Article
  8. Article
  9. Article
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  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
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  19. Review
  20. Some G protein heterotrimers physically dissociate in living cells.Proceedings of the National Academy of Sciences of the United States of America · 2006
    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

2 authors at 1 institution in 1 country.

U QuittererInstitut für Pharmakologie und Toxikologie der Universität Würzburg, Versbacher Strasse 9, 97078 Würzburg, Germany.
M J Lohse
University of Würzburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Activation of Galpha(i)-coupled receptors often causes enhancement of the inositol phosphate signal triggered by Galpha(q)-coupled receptors. To investigate the mechanism of this synergistic receptor crosstalk, we studied the Galpha(i)-coupled adenosine A(1) and alpha(2C) adrenergic receptors and the Galpha(q)-coupled bradykinin B(2) and a UTP-preferring P2Y receptor. Stimulation of either Galpha(i)-coupled receptor expressed in COS cells increased the potency and the efficacy of inositol phosphate production by bradykinin or UTP. Likewise, overexpression of Gbeta(1)gamma(2) resulted in a similar increase in potency and efficacy of bradykinin or UTP. In contrast, these stimuli did not affect the potency of direct activators of Galpha(q); a truncated Gbeta(3) mutant had no effect on the receptor-generated signals whereas signals generated at the G-protein level were still enhanced. This suggests that the Gbetagamma-mediated signal enhancement occurs at the receptor level. Almost all possible combinations of Gbeta(1-3) with Ggamma(2-7) were equally effective in enhancing the signals of the B(2) and a UTP-preferring P2Y receptor, indicating a very broad specificity of this synergism. The enhancement of the bradykinin signal by (i) Galpha(i)-activating receptor ligands or (ii) cotransfection of Gbetagamma was suppressed when the B(2) receptor was replaced by a B(2)Gbeta(2) fusion protein. Gbetagamma enhanced the B(2) receptor-stimulated activation of G-proteins as determined by GTPgammaS-induced decrease in high affinity agonist binding and by B(2) receptor-enhanced [(35)S]GTPgammaS binding. These findings support the concept that Gbetagamma exchange between Galpha(i)- and Galpha(q)-coupled receptors mediates this type of receptor crosstalk.

Indexed as

AnimalsCalciumCOS CellsDose-Response Relationship, DrugGTP-Binding ProteinsImmunoblottingInositol PhosphatesModels, BiologicalMutagenesisReceptor, Bradykinin B2Receptor Cross-TalkReceptors, Adrenergic, beta-2Receptors, BradykininRecombinant Fusion ProteinsSignal TransductionTime FactorsCalciumGTP-Binding ProteinsInositol PhosphatesReceptor, Bradykinin B2Receptors, Adrenergic, beta-2Receptors, BradykininRecombinant Fusion ProteinsType C PhospholipasesUridine Triphosphate

Identifiers

PMID10485876
PMCPMC17933
OpenAlexW1663699868

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.