Evidence map›Paper›PMID 10990530›Full record

ArticleThe Journal of physiology2000

Interaction between G proteins and accessory subunits in the regulation of 1B calcium channels in Xenopus oocytes.

C Cantí, Y Bogdanov, A C Dolphin

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The Journal of physiology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

26 citing papers in PubMed, 69 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Presynaptic Calcium Channels.International journal of molecular sciences · 2019
    Review
  5. Article
  6. Review
  7. Review
  8. Rim1 modulates direct G-protein regulation of Ca(v)2.2 channels.Pflugers Archiv : European journal of physiology · 2011
    Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Origin of the voltage dependence of G-protein regulation of P/Q-type Ca2+ channels.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2008
    Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  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

3 authors at 1 institution in 1 country.

C CantíDepartment of Pharmacology, University College London, Gower Street, London WC1E 6BT, UK. c.canti@ucl.ac.uk
Y Bogdanov
A C Dolphin
University College London · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

The accessory beta subunits of voltage-dependent Ca2+ channels (VDCCs) have been shown to regulate their biophysical properties and have also been suggested to antagonise the G protein inhibition of N-type (alpha1B), P/Q-type (alpha1A) and alpha1E channels. Here we have examined the voltage-dependent involvement of the four neuronal isoforms (beta1b, beta2a, beta3 and beta4) in the process of G protein modulation of alpha1B Ca2+ channels. All beta subunits hyperpolarized alpha1B current activation, and all antagonised the G protein-mediated depolarisation of current activation. However, except in the case of beta2a, there was no generalised reduction by beta subunits in the maximal extent of receptor-mediated inhibition of alpha1B current. In addition, all VDCC beta subunits enhanced the rate of current facilitation at +100 mV, for both receptor-mediated and tonic modulation. The rank order for enhancement of facilitation rate was beta3 > beta4 > beta1b > beta2a. In contrast, the amount of voltage-dependent facilitation during tonic modulation was reduced by beta subunit co-expression, despite the fact that the apparent Gbetagamma dissociation rate at +100 mV was enhanced by beta subunits to a similar level as for agonist-induced modulation. Our data provide evidence that G protein activation antagonises Ca2+-channel beta subunit-induced hyperpolarisation of current activation. Conversely, co-expression of all beta subunits increases the apparent Gbetagamma dimer dissociation rate during a depolarising prepulse. This latter feature suggests the co-existence of bound Ca2+-channel beta subunits and Gbetagamma dimers on the alpha1B subunits. Future work will determine how the interaction between Gbetagamma dimers and Ca2+-channel beta subunits with alpha1B results in a functional antagonism at the molecular level.

Indexed as

AnimalsCalcium ChannelsDNADopamine AgonistsElectrophysiologyGTP-Binding ProteinsKineticsMembrane PotentialsOocytesPatch-Clamp TechniquesQuinpiroleRatsReceptors, Dopamine D2Xenopus laevisCalcium ChannelsDNADopamine AgonistsGTP-Binding ProteinsQuinpiroleReceptors, Dopamine D2

Identifiers

PMID10990530
PMCPMC2270102
OpenAlexW2010831941

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.