Evidence map›Paper›PMID 19561088›Full record

ArticleThe Journal of biological chemistry2009

Intersubunit coupling in the pore of BK channels.

Ying Wu, Yu Xiong, Sheng Wang, Hong Yi, Hui Li, Na Pan, Frank T Horrigan, Yingliang Wu, Jiuping Ding

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing 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

23 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Atomic determinants of BK channel activation by polyunsaturated fatty acids.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  10. Article
  11. Article
  12. Article
  13. BK channel opening involves side-chain reorientation of multiple deep-pore residues.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
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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

9 authors.

Ying WuKey Laboratory of Molecular Biophysics, Huazhong University of Science and Technology, the Ministry of Education, Wuhan, Hubei 430074, China.
Yu Xiong
Sheng Wang
Hong Yi
Hui Li
Na Pan
Frank T Horrigan
Yingliang Wu
Jiuping Ding

Funding

Allosteric mechanisms of CA-activated K channel gatingR01NS042901 · NINDS · UNIVERSITY OF PENNSYLVANIA · PI HORRIGAN, FRANK T · 2001 to 2011
$3.0M
NINDS NIH HHS NS042901NINDS NIH HHS R01 NS042901
6 · The paper itself

Abstract

The structural basis underlying the gating of large conductance Ca(2+)-activated K(+) (BK) channels remains elusive. We found that substitution of Leu-312 in the S6 transmembrane segment of mSlo1 BK channels with hydrophilic amino acids of smaller side-chain volume favored the open state. The sensitivities of channels to calcium and voltage were modified by some mutations and completely abolished by others. Interpretation of the results in terms of an allosteric model suggests that the calcium-insensitive mutants greatly destabilize the closed relative to the open conformation and may also disrupt the allosteric coupling between Ca(2+) or voltage sensors and the gate. Some Phe-315 mutations also favor the open state, suggesting that Leu-312 and Phe-315 may interact in the closed state, forming a major energy barrier that the channel has to overcome to open. Homology modeling and molecular dynamic simulations further support that the side chain of Leu-312 can couple strongly with the aromatic ring of Phe-315 in neighboring subunits (L-F coupling) to maintain the channel closed. Additionally, single-channel recordings indicate that the calcium-insensitive mutants, whose kinetics can be approximately characterized by a two-state closed-open (C-O) model, exhibit nearly 100% open probability under physiological conditions without alterations in single-channel conductance. These findings provide a basis for understanding the structure and gating of the BK channel pore.

Indexed as

Amino Acid SubstitutionAnimalsCalciumHumansIon Channel GatingKineticsLarge-Conductance Calcium-Activated Potassium Channel alpha SubunitsLarge-Conductance Calcium-Activated Potassium ChannelsMiceMolecular ConformationProtein ConformationCalciumKcnma1 protein, mouseLarge-Conductance Calcium-Activated Potassium Channel alpha SubunitsLarge-Conductance Calcium-Activated Potassium Channels

Identifiers

PMID19561088
PMCPMC2749109

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.