Evidence map›Paper›PMID 10358108›Full record

ArticleThe Journal of physiology1999

Auxiliary subunits operate as a molecular switch in determining gating behaviour of the unitary N-type Ca2+ channel current in Xenopus oocytes.

M Wakamori, G Mikala, Y Mori

Abstract 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 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
–field-weighted citation impact
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

28 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. Neuronal αPflugers Archiv : European journal of physiology · 2020
    Review
  5. CACHD1 is an α2δ-Like Protein That Modulates CaThe Journal of neuroscience : the official journal of the Society for Neuroscience · 2018
    Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Review
  11. Functional exofacially tagged N-type calcium channels elucidate the interaction with auxiliary α2δ-1 subunits.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  12. Article
  13. Article
  14. Review
  15. The role of a voltage-dependent Ca2+ channel intracellular linker: a structure-function analysis.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2012
    Article
  16. Review
  17. Article
  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.

M WakamoriDepartment of Information Physiology, National Institute for Physiological Sciences, Okazaki, Aichi 444-8585, Japan.
G Mikala
Y Mori

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

1. We systematically examined the biophysical properties of omega-conotoxin GVIA-sensitive neuronal N-type channels composed of various combinations of the alpha1B, alpha2/delta and beta1b subunits in Xenopus oocytes. 2. Whole-cell recordings demonstrated that coexpression of the beta1b subunit decelerated inactivation, whereas the alpha2/delta accelerated both activation and inactivation, and cancelled the kinetic effects of the beta1b. The alpha2/delta and the beta1b controlled voltage dependence of activation differently: the beta1b significantly shifted the current-voltage relationship towards the hyperpolarizing direction; however, the alpha2/delta shifted the relationship only slightly in the depolarizing direction. The extent of voltage-dependent inactivation was modified solely by the beta1b. 3. Unitary currents measured using a cell-attached patch showed stable patterns of opening that were markedly different among subunit combinations in their kinetic parameters. The alpha2/delta and the beta1b subunits also acted antagonistically in regulating gating patterns of unitary N-type channels. Open time was shortened by the alpha2/delta, while the fraction of long opening was enhanced by the beta1b. The alpha2/delta decreased opening probability (Po), while the beta1b increased Po. alpha1Balpha2/deltabeta1b produced unitary activity with an open time distribution value in between those of alpha1Balpha2/delta and alpha1Bbeta1b. However, both the alpha2/delta and the beta1b subunits reduced the number of null traces. 4. These results suggest that the auxiliary subunits alone and in combination contribute differently in forming gating apparatuses in the N-type channel, raising the possibility that subunit interaction contributes to the generation of functional diversity of N-type channels in native neuronal preparations also.

Indexed as

Calcium Channels, N-TypeAnimalsCalcium Channel BlockersCalcium ChannelsFemaleGene Expression RegulationIon Channel GatingKineticsMacromolecular SubstancesMembrane PotentialsNeuronsomega-Conotoxin GVIAOocytesPeptidesProtein MultimerizationRecombinant ProteinsCalcium Channel BlockersCalcium ChannelsCalcium Channels, N-TypeMacromolecular Substancesomega-Conotoxin GVIAPeptidesRecombinant Proteins

Identifiers

PMID10358108
PMCPMC2269381

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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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.