Evidence map›Paper›PMID 18567635›Full record

ArticleBiophysical journal2008

Voltage-dependent C-type inactivation in a constitutively open K+ channel.

Gianina Panaghie, Kerry Purtell, Kwok-Keung Tai, Geoffrey W Abbott

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing 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

18 citing papers in PubMed, 21 citations in OpenAlex.

  1. Mechanism of external K+ sensitivity of KCNQ1 channels.The Journal of general physiology · 2023
    Article
  2. KCNQ Potassium Channels as Targets of Botanical Folk Medicines.Annual review of pharmacology and toxicology · 2022
    Review
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  10. Closed state-coupled C-type inactivation in BK channels.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  11. Review
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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

4 authors at 2 institutions in 1 country.

Gianina PanaghieGreenberg Division of Cardiology, Department of Medicine, Cornell University, Weill Medical College, New York, New York, USA.
Kerry Purtell
Kwok-Keung Tai
Geoffrey W Abbott
Cornell University · USLong Beach Memorial Medical Center · US

Funding

K+ channel trafficking and modulation in MinK and MiRP1R01HL079275 · NHLBI · WEILL MEDICAL COLL OF CORNELL UNIV · PI ABBOTT, GEOFFREY W · 2005 to 2015
$4.6M
NHLBI NIH HHS R01 HL079275
6 · The paper itself

Abstract

Most voltage-gated potassium (Kv) channels undergo C-type inactivation during sustained depolarization. The voltage dependence and other mechanistic aspects of this process are debated, and difficult to elucidate because of concomitant voltage-dependent activation. Here, we demonstrate that MinK-KCNQ1 (I(Ks)) channels with an S6-domain mutation, F340W in KCNQ1, exhibit constitutive activation but voltage-dependent C-type inactivation. F340W-I(Ks) inactivation was sensitive to extracellular cation concentration and species, and it altered ion selectivity, suggestive of pore constriction. The rate and extent of F340W-I(Ks) inactivation and recovery from inactivation were voltage-dependent with physiologic intracellular ion concentrations, and in the absence or presence of external K(+), with an estimated gating charge, z(i), of approximately 1. Finally, double-mutant channels with a single S4 charge neutralization (R231A,F340W-I(Ks)) exhibited constitutive C-type inactivation. The results suggest that F340W-I(Ks) channels exhibit voltage-dependent C-type inactivation involving S4, without the necessity for voltage-dependent opening, allosteric coupling to voltage-dependent S6 transitions occurring during channel opening, or voltage-dependent changes in ion occupancy. The data also identify F340 as a critical hub for KCNQ1 gating processes and their modulation by MinK, and present a unique system for further mechanistic studies of the role of coupling of C-type inactivation to S4 movement, without contamination from voltage-dependent activation.

Indexed as

Ion Channel GatingAmino Acid SequenceAnimalsCell Membrane PermeabilityElectric ConductivityExtracellular SpaceHumansKCNQ1 Potassium ChannelKineticsMolecular Sequence DataMutant ProteinsMutationPorosityProtein Structure, TertiarySubstrate SpecificityXenopus laevisKCNQ1 Potassium ChannelMutant Proteins

Identifiers

PMID18567635
PMCPMC2527255
OpenAlexW2026815132

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.