Evidence map›Paper›PMID 24367115›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2014

BK channel opening involves side-chain reorientation of multiple deep-pore residues.

Xixi Chen, Jiusheng Yan, Richard W Aldrich

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing 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

36 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. Coupling of CaProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  17. Large-conductance CaProceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  18. Hydrophobic gating in BK channels.Nature communications · 2018
    Article
  19. Article
  20. Review
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.

Xixi ChenDepartment of Neuroscience and Center for Learning and Memory, The University of Texas at Austin, Austin, TX 78712.
Jiusheng Yan
Richard W Aldrich

Funding

Mechanisms of Calcium-Calmodulin Mediated Ion Channel GatingR01NS077821 · NINDS · UNIVERSITY OF TEXAS AT AUSTIN · PI ALDRICH, RICHARD · 2011 to 2021
$4.7M
BK channel regulation by auxiliary LRR proteinsR01NS078152 · NINDS · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI YAN, JIUSHENG · 2012 to 2022
$3.5M
A screen for peptides that alter BK channel-mediated alcohol intoxicationR01AA020992 · NIAAA · UNIVERSITY OF TEXAS AT AUSTIN · PI ALDRICH, RICHARD, MIHIC, S JOHN · 2012 to 2016
$2.0M
NIAAA NIH HHS AA020992NIAAA NIH HHS R01 AA020992NINDS NIH HHS NS077821NINDS NIH HHS NS078152NINDS NIH HHS R01 NS077821NINDS NIH HHS R01 NS078152
6 · The paper itself

Abstract

Three deep-pore locations, L312, A313, and A316, were identified in a scanning mutagenesis study of the BK (Ca(2+)-activated, large-conductance K(+)) channel S6 pore, where single aspartate substitutions led to constitutively open mutant channels (L312D, A313D, and A316D). To understand the mechanisms of the constitutive openness of these mutant channels, we individually mutated these three sites into the other 18 amino acids. We found that charged or polar side-chain substitutions at each of the sites resulted in constitutively open mutant BK channels, with high open probability at negative voltages, as well as a loss of voltage and Ca(2+) dependence. Given the fact that multiple pore residues in BK displayed side-chain hydrophilicity-dependent constitutive openness, we propose that BK channel opening involves structural rearrangement of the deep-pore region, where multiple residues undergo conformational changes that may increase the exposure of their side chains to the polar environment of the pore.

Indexed as

Ion Channel GatingProtein ConformationAmino Acid SequenceCalciumElectrophysiological PhenomenaHEK293 CellsHumansLarge-Conductance Calcium-Activated Potassium ChannelsMolecular Sequence DataMutagenesis, Site-DirectedMutationPhenotypeProtein BindingSequence Homology, Amino AcidCalciumLarge-Conductance Calcium-Activated Potassium Channelsgatingion channel porestructure–function

Identifiers

PMID24367115
PMCPMC3890798

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.