Evidence map›Paper›PMID 21576375›Full record

ArticleThe Journal of general physiology2011

Low resistance, large dimension entrance to the inner cavity of BK channels determined by changing side-chain volume.

Yanyan Geng, Xiaowei Niu, Karl L Magleby

Abstract read
In one paragraph

Article in The Journal of general physiology, 2011. 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
–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

22 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Queueing arrival and release mechanism for KThe journal of physiological sciences : JPS · 2019
    Article
  6. Hydrophobic gating in BK channels.Nature communications · 2018
    Article
  7. Review
  8. Article
  9. Pore size matters for potassium channel conductance.The Journal of general physiology · 2016
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. 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.

Yanyan GengDepartment of Physiology and Biophysics, University of Miami Miller School of Medicine, FL 33136, USA. ygeng@-med.miami.edu
Xiaowei Niu
Karl L Magleby

Funding

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

Abstract

Large-conductance Ca(2+)- and voltage-activated K(+) (BK) channels have the largest conductance (250-300 pS) of all K(+)-selective channels. Yet, the contributions of the various parts of the ion conduction pathway to the conductance are not known. Here, we examine the contribution of the entrance to the inner cavity to the large conductance. Residues at E321/E324 on each of the four α subunits encircle the entrance to the inner cavity. To determine if 321/324 is accessible from the inner conduction pathway, we measured single-channel current amplitudes before and after exposure and wash of thiol reagents to the intracellular side of E321C and E324C channels. MPA(-) increased currents and MTSET(+) decreased currents, with no difference between positions 321 and 324, indicating that side chains at 321/324 are accessible from the inner conduction pathway and have equivalent effects on conductance. For neutral amino acids, decreasing the size of the entrance to the inner cavity by substituting large side-chain amino acids at 321/324 decreased outward single-channel conductance, whereas increasing the size of the entrance with smaller side-chain substitutions had little effect. Reductions in outward conductance were negated by high [K(+)](i). Substitutions had little effect on inward conductance. Fitting plots of conductance versus side-chain volume with a model consisting of one variable and one fixed resistor in series indicated an effective diameter and length of the entrance to the inner cavity for wild-type channels of 17.7 and 5.6 Å, respectively, with the resistance of the entrance ∼7% of the total resistance of the conduction pathway. The estimated dimensions are consistent with the structure of MthK, an archaeal homologue to BK channels. Our observations suggest that BK channels have a low resistance, large entrance to the inner cavity, with the entrance being as large as necessary to not limit current, but not much larger.

Indexed as

Amino Acid SequenceAnimalsCloning, MolecularDNA-Binding ProteinsElectrochemistryIon TransportLarge-Conductance Calcium-Activated Potassium ChannelsModels, MolecularOocytesPotassiumProtein ConformationViral ProteinsDNA-Binding ProteinsLarge-Conductance Calcium-Activated Potassium ChannelsMuB protein, Enterobacteria phage MuPotassiumViral Proteins

Identifiers

PMID21576375
PMCPMC3105516

What OpenQuestion holds

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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.