Evidence map›Paper›PMID 12893878›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2003

Beta1 subunits facilitate gating of BK channels by acting through the Ca2+, but not the Mg2+, activating mechanisms.

Xiang Qian, Karl L Magleby

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

22 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
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  5. Molecular mechanism underlying β1 regulation in voltage- and calcium-activated potassium (BK) channels.Proceedings of the National Academy of Sciences of the United States of America · 2015
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  9. Modulation of BK channel voltage gating by different auxiliary β subunits.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  10. Article
  11. Article
  12. Article
  13. MiRP3 acts as an accessory subunit with the BK potassium channel.American journal of physiology. Renal physiology · 2008
    Article
  14. Effects of Atractylodes macrocephala on the cytomembrane Ca2+-activated K+ currents in cells of human pregnant myometrial smooth muscles.Journal of Huazhong University of Science and Technology. Medical sciences = Hua zhong ke ji da xue xue bao. Yi xue Ying De wen ban = Huazhong keji daxue xuebao. Yixue Yingdewen ban · 2008
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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.

Xiang QianDepartment of Physiology and Biophysics, University of Miami School of Medicine, 1600 Northwest 10th Avenue, Miami, FL 33136, USA.
Karl L Magleby
University of Miami · US

Funding

MECHANISMS OF IONIC CHANNEL ACTIVITYR01AR032805 · NIAMS · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI MAGLEBY, KARL L · 1986 to 2012
$4.3M
MECHANISMS OF IONIC CHANNEL ACTIVITYR37AR032805 · NIAMS · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI MAGLEBY, KARL L · 1988 to 1997
–
NIAMS NIH HHS AR 32805NIAMS NIH HHS R01 AR032805
6 · The paper itself

Abstract

The beta1 subunit of BK (large conductance Ca2+ and voltage-activated K+) channels is essential for many key physiological processes, such as controlling the contraction of smooth muscle and the tuning of hair cells in the cochlea. Although it is known that the beta1 subunit greatly increases the open probability of BK channels, little is known about its mechanism of action. We now explore this mechanism by using channels in which the Ca2+- and Mg2+-dependent activating mechanisms have been disrupted by mutating three sites to remove the Ca2+ and Mg2+ sensitivity. We find that the presence of the beta1 subunit partially restores Ca2+ sensitivity to the triply mutated channels, but not the Mg2+ sensitivity. We also find that the beta1 subunit has no effect on the Mg2+ sensitivity of WT BK channels, in contrast to its pronounced effect of increasing the apparent Ca2+ sensitivity. These observations suggest that the beta1 subunit increases open probability by working through the Ca2+-dependent, rather than Mg2+-dependent, activating mechanisms, and that the action of the beta1 subunit is not directly on the Ca2+ binding sites, but on the allosteric machinery coupling the sites to the gate. The differential effects of the beta1 subunit on the Ca2+ and Mg2+ activation of the channel suggest that these processes act separately. Finally, we show that Mgi2+ inhibits, rather than activates, BK channels in the presence of the beta1 subunit for intermediate levels of Cai2+. This Mg2+ inhibition in the presence of the beta1 subunit provides an additional regulatory mechanism of BK channel activity.

Indexed as

AnimalsBinding SitesCalciumFemaleHumansIn Vitro TechniquesIon Channel GatingKineticsLarge-Conductance Calcium-Activated Potassium ChannelsMagnesiumMiceMutagenesis, Site-DirectedOocytesPotassium Channels, Calcium-ActivatedProtein SubunitsRecombinant ProteinsCalciumLarge-Conductance Calcium-Activated Potassium ChannelsMagnesiumPotassium Channels, Calcium-ActivatedProtein SubunitsRecombinant Proteins

Identifiers

PMID12893878
PMCPMC187764
OpenAlexW2104846898

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.