Evidence map›Paper›PMID 10332086›Full record

ArticleThe Journal of physiology1999

New roles for RGS2, 5 and 8 on the ratio-dependent modulation of recombinant GIRK channels expressed in Xenopus oocytes.

S Herlitze, J P Ruppersberg, M D Mark

Open access · greenAbstract read
In one paragraph

Article in The Journal of physiology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.8field-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

19 citing papers in PubMed, 53 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. The selective antagonist EPPTB reveals TAAR1-mediated regulatory mechanisms in dopaminergic neurons of the mesolimbic system.Proceedings of the National Academy of Sciences of the United States of America · 2009
    Article
  5. Review
  6. Abscisic acid regulation of guard-cell K+ and anion channels in Gbeta- and RGS-deficient Arabidopsis lines.Proceedings of the National Academy of Sciences of the United States of America · 2008
    Article
  7. Article
  8. Review
  9. Gene-trapped mouse embryonic stem cell-derived cardiac myocytes and human genetics implicate AKAP10 in heart rhythm regulation.Proceedings of the National Academy of Sciences of the United States of America · 2007
    Article
  10. Review
  11. Article
  12. G-protein signaling: back to the future.Cellular and molecular life sciences : CMLS · 2005
    Review
  13. Article
  14. Article
  15. Article
  16. Article
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  18. Article
  19. 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

3 authors at 1 institution in 1 country.

S HerlitzeDepartment of Physiology II, University of Tuebingen, Ob dem Himmelreich 7, 72074 Tuebingen, Germany.
J P Ruppersberg
M D Mark
University of Tübingen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

1. The activation of G protein-regulated inward rectifying potassium (GIRK) channels is modulated by G protein-coupled receptors (GPCRs) via the G protein betagamma subunits and is accelerated by regulators of G protein signalling (RGS). In the present study we investigated the ratio dependence of receptor-mediated activation and deactivation and the influence of new members of the RGS protein family on GIRK currents by coexpressing the recombinant protein subunits in Xenopus oocytes and further analysis of the whole cell currents. 2. The activation of GIRK channels by the muscarinic acetylcholine receptor M2 (M2 mAChR) is strongly dependent on the ratio of receptor to channel in Xenopus oocytes. The increase and on-rate of the amplified current is affected by this ratio. An excess of receptor over channel is necessary for current amplification, while the reverse excess of channel over receptor abolishes the effect. 3. The speed of receptor-mediated activation of GIRK currents is accelerated for a high ratio of receptor to channel, while the time of deactivation is independent of this ratio. 4. Coexpression of RGS2, 5 and 8 accelerates the speed for ACh-mediated activation and deactivation of GIRK1/2 and GIRK1/4 currents. Thereby the receptor/channel/RGS ratio determines the amount of current amplification. 5. Bordetella pertussis toxin completely abolished ACh-mediated current amplification of GIRK channels coexpressed with or without RGS2. 6. Two single point mutations in the RGS2 protein (RGS2(N109S) and RGS2(L180F)) reduced the acceleration of current amplification after ACh application on GIRK1/4 channels compared with RGS2 wild-type protein.

Indexed as

Potassium Channels, Inwardly RectifyingRGS ProteinsXenopus ProteinsAmino Acid SequenceAnimalsElectric ConductivityFemaleGTPase-Activating ProteinsGTP-Binding ProteinsMiceMolecular Sequence DataOocytesPertussis ToxinPoint MutationPotassium ChannelsProteinsGTPase-Activating ProteinsGTP-Binding ProteinsPertussis ToxinPotassium ChannelsPotassium Channels, Inwardly RectifyingProteinsReceptors, MuscarinicRecombinant ProteinsRgs2 protein, mouseRGS4 proteinRgs5 protein, mouseRgs5 protein, ratRgs5 protein, XenopusRGS ProteinsVirulence Factors, BordetellaXenopus Proteins

Identifiers

PMID10332086
PMCPMC2269356
OpenAlexW1996501707

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.