Evidence map›Paper›PMID 18461166›Full record

ArticlePloS one2008

Lysine-rich extracellular rings formed by hbeta2 subunits confer the outward rectification of BK channels.

Maorong Chen, Geliang Gan, Ying Wu, Lu Wang, Yingliang Wu, Jiuping Ding

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
0.6field-weighted citation impact, top 34% 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

15 citing papers in PubMed, 19 citations in OpenAlex.

  1. An extracellular scaffolding complex confers unusual rectification upon an ionotropic acetylcholine receptor inProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  2. Effect of an autism-associatedCurrent research in physiology · 2022
    Article
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  4. Review
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  12. Modulation of BK channel voltage gating by different auxiliary β subunits.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  13. Article
  14. Article
  15. The dipeptidyl-peptidase-like protein DPP6 determines the unitary conductance of neuronal Kv4.2 channels.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2009
    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

6 authors at 2 institutions in 1 country.

Maorong ChenKey Laboratory of Molecular Biophysics, Huazhong University of Science and Technology, Ministry of Education, College of Life Science and Technology, Wuhan, Hubei, China.
Geliang Gan
Ying Wu
Lu Wang
Yingliang Wu
Jiuping Ding
Huazhong University of Science and Technology · CNWuhan University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The auxiliary beta subunits of large-conductance Ca(2+)-activated K(+) (BK) channels greatly contribute to the diversity of BK (mSlo1 alpha) channels, which is fundamental to the adequate function in many tissues. Here we describe a functional element of the extracellular segment of hbeta2 auxiliary subunits that acts as the positively charged rings to modify the BK channel conductance. Four consecutive lysines of the hbeta2 extracellular loop, which reside sufficiently close to the extracellular entryway of the pore, constitute three positively charged rings. These rings can decrease the extracellular K(+) concentration and prevent the Charybdotoxin (ChTX) from approaching the extracellular entrance of channels through electrostatic mechanism, leading to the reduction of K(+) inflow or the outward rectification of BK channels. Our results demonstrate that the lysine rings formed by the hbeta2 auxiliary subunits influences the inward current of BK channels, providing a mechanism by which current can be rapidly diminished during cellular repolarization. Furthermore, this study will be helpful to understand the functional diversity of BK channels contributed by different auxiliary beta subunits.

Indexed as

Amino Acid SequenceAnimalsCalciumCharybdotoxinEpitopesLarge-Conductance Calcium-Activated Potassium Channel alpha SubunitsLarge-Conductance Calcium-Activated Potassium Channel beta SubunitsLarge-Conductance Calcium-Activated Potassium ChannelsLysinePatch-Clamp TechniquesPeptide FragmentsPotassiumProtein SubunitsStatic ElectricityCalciumCharybdotoxinEpitopesLarge-Conductance Calcium-Activated Potassium Channel alpha SubunitsLarge-Conductance Calcium-Activated Potassium Channel beta SubunitsLarge-Conductance Calcium-Activated Potassium ChannelsLysinePeptide FragmentsPotassiumProtein Subunits

Identifiers

PMID18461166
PMCPMC2346552
OpenAlexW1969880518

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.