Evidence map›Paper›PMID 16103277›Full record

ArticleThe Journal of general physiology2005

The NH2 terminus of RCK1 domain regulates Ca2+-dependent BK(Ca) channel gating.

Gayathri Krishnamoorthy, Jingyi Shi, David Sept, Jianmin Cui

Abstract read
In one paragraph

Article in The Journal of general physiology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing 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

21 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Coupling of CaProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  5. Effects of Single Nucleotide Polymorphisms in HumanFrontiers in molecular neuroscience · 2019
    Article
  6. Review
  7. Pore size matters for potassium channel conductance.The Journal of general physiology · 2016
    Review
  8. Article
  9. Review
  10. Single-channel kinetics of BK (Slo1) channels.Frontiers in physiology · 2014
    Review
  11. The relationship between duration of initial alcohol exposure and persistence of molecular tolerance is markedly nonlinear.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2011
    Article
  12. Modulation of BK channel gating by the ß2 subunit involves both membrane-spanning and cytoplasmic domains of Slo1.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2010
    Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Mg2+ mediates interaction between the voltage sensor and cytosolic domain to activate BK channels.Proceedings of the National Academy of Sciences of the United States of America · 2007
    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

4 authors.

Gayathri KrishnamoorthyDepartment of Biomedical Engineering, Case Western Reserve University, Cleveland, OH 44106, USA.
Jingyi Shi
David Sept
Jianmin Cui

Funding

Ca2+ Dependent K+ Channels: Allosteric GatingR01HL070393 · NHLBI · WASHINGTON UNIVERSITY · PI CUI, JIANMIN · 2002 to 2015
$4.9M
NHLBI NIH HHS R01 HL070393NHLBI NIH HHS R01-HL70393
6 · The paper itself

Abstract

Large conductance, voltage- and Ca2+-activated K+ (BK(Ca)) channels regulate blood vessel tone, synaptic transmission, and hearing owing to dual activation by membrane depolarization and intracellular Ca2+. Similar to an archeon Ca2+-activated K+ channel, MthK, each of four alpha subunits of BK(Ca) may contain two cytosolic RCK domains and eight of which may form a gating ring. The structure of the MthK channel suggests that the RCK domains reorient with one another upon Ca2+ binding to change the gating ring conformation and open the activation gate. Here we report that the conformational changes of the NH2 terminus of RCK1 (AC region) modulate BK(Ca) gating. Such modulation depends on Ca2+ occupancy and activation states, but is not directly related to the Ca2+ binding sites. These results demonstrate that AC region is important in the allosteric coupling between Ca2+ binding and channel opening. Thus, the conformational changes of the AC region within each RCK domain is likely to be an important step in addition to the reorientation of RCK domains leading to the opening of the BK(Ca) activation gate. Our observations are consistent with a mechanism for Ca2+-dependent activation of BK(Ca) channels such that the AC region inhibits channel activation when the channel is at the closed state in the absence of Ca2+; Ca2+ binding and depolarization relieve this inhibition.

Indexed as

Ion Channel GatingAllosteric RegulationAmino Acid SequenceAnimalsBinding SitesCalciumCloning, MolecularConserved SequenceDose-Response Relationship, DrugLarge-Conductance Calcium-Activated Potassium ChannelsMembrane PotentialsMolecular Sequence DataMutationOocytesPotassium Channels, Calcium-ActivatedProtein Structure, TertiaryCalciumLarge-Conductance Calcium-Activated Potassium ChannelsPotassium Channels, Calcium-Activated

Identifiers

PMID16103277
PMCPMC2266574

What OpenQuestion holds

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LicenceCC BY-NC-SA
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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.