Evidence map›Paper›PMID 24067659›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

Properties of Slo1 K+ channels with and without the gating ring.

Gonzalo Budelli, Yanyan Geng, Alice Butler, Karl L Magleby, Lawrence Salkoff

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

40 citing papers in PubMed, 58 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Redox-dependent CdBiophysical journal · 2024
    Article
  7. Article
  8. Review
  9. BK Channelopathies andAnnual review of physiology · 2024
    Review
  10. Article
  11. Pharmacological Evidence Suggests That Slo3 Channel Is the Principal KInternational journal of molecular sciences · 2023
    Article
  12. Article
  13. Regulation of Neurotransmitter Release by KAdvances in neurobiology · 2023
    Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Coupling of CaProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  20. The action of a BK channel opener.The Journal of general physiology · 2020
    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

5 authors at 2 institutions in 1 country.

Gonzalo BudelliDepartments of Anatomy and Neurobiology and Genetics, Washington University School of Medicine in St. Louis, St. Louis, MO 63110.
Yanyan Geng
Alice Butler
Karl L Magleby
Lawrence Salkoff
University of Miami · USWashington University in St. Louis · 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 AR032805NIAMS NIH HHS R01 AR032805NINDS NIH HHS NS0661871
6 · The paper itself

Abstract

High-conductance Ca(2+)- and voltage-activated K(+) (Slo1 or BK) channels (KCNMA1) play key roles in many physiological processes. The structure of the Slo1 channel has two functional domains, a core consisting of four voltage sensors controlling an ion-conducting pore, and a larger tail that forms an intracellular gating ring thought to confer Ca(2+) and Mg(2+) sensitivity as well as sensitivity to a host of other intracellular factors. Although the modular structure of the Slo1 channel is known, the functional properties of the core and the allosteric interactions between core and tail are poorly understood because it has not been possible to study the core in the absence of the gating ring. To address these questions, we developed constructs that allow functional cores of Slo1 channels to be expressed by replacing the 827-amino acid gating ring with short tails of either 74 or 11 amino acids. Recorded currents from these constructs reveals that the gating ring is not required for either expression or gating of the core. Voltage activation is retained after the gating ring is replaced, but all Ca(2+)- and Mg(2+)-dependent gating is lost. Replacing the gating ring also right-shifts the conductance-voltage relation, decreases mean open-channel and burst duration by about sixfold, and reduces apparent mean single-channel conductance by about 30%. These results show that the gating ring is not required for voltage activation but is required for Ca(2+) and Mg(2+) activation. They also suggest possible actions of the unliganded (passive) gating ring or added short tails on the core.

Indexed as

AnimalsCalciumHumansIon Channel GatingKineticsKv1.4 Potassium ChannelLarge-Conductance Calcium-Activated Potassium Channel alpha SubunitsMagnesiumMiceMutagenesis, Site-DirectedOligonucleotidesOocytesPatch-Clamp TechniquesPeptidesTetraethylammoniumXenopusCalciumiberiotoxinKCNMA1 protein, humanKv1.4 Potassium ChannelLarge-Conductance Calcium-Activated Potassium Channel alpha SubunitsMagnesiumOligonucleotidesPeptidesTetraethylammoniumBK channeliberiotoxinKv1.4tetraethylammoniumβ1 subunit

Identifiers

PMID24067659
PMCPMC3799338
OpenAlexW2077857264

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.