Evidence map›Paper›PMID 27317659›Full record

ArticleThe Journal of biological chemistry2016

Tyrosine Residues from the S4-S5 Linker of Kv11.1 Channels Are Critical for Slow Deactivation.

Chai-Ann Ng, Andrée E Gravel, Matthew D Perry, Alexandre A Arnold, Isabelle Marcotte, Jamie I Vandenberg

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. 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

6 authors.

Chai-Ann NgFrom the Victor Chang Cardiac Research Institute, 405 Liverpool Street, Darlinghurst and the St. Vincent's Clinical School, University of New South Wales, Victoria Street, Darlinghurst, New South Wales 2010, Australia and.ORCID 0000-0002-3120-5450
Andrée E Gravelthe Department of Chemistry, Université du Québec à Montréal, Montreal H3C 3P8, Québec, Canada.
Matthew D PerryFrom the Victor Chang Cardiac Research Institute, 405 Liverpool Street, Darlinghurst and the St. Vincent's Clinical School, University of New South Wales, Victoria Street, Darlinghurst, New South Wales 2010, Australia and.
Alexandre A Arnoldthe Department of Chemistry, Université du Québec à Montréal, Montreal H3C 3P8, Québec, Canada.
Isabelle Marcottethe Department of Chemistry, Université du Québec à Montréal, Montreal H3C 3P8, Québec, Canada marcotte.isabelle@uqam.ca.
Jamie I VandenbergFrom the Victor Chang Cardiac Research Institute, 405 Liverpool Street, Darlinghurst and the St. Vincent's Clinical School, University of New South Wales, Victoria Street, Darlinghurst, New South Wales 2010, Australia and j.vandenberg@victorchang.edu.au.ORCID 0000-0002-3859-3716

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Slow deactivation of Kv11.1 channels is critical for its function in the heart. The S4-S5 linker, which joins the voltage sensor and pore domains, plays a critical role in this slow deactivation gating. Here, we use NMR spectroscopy to identify the membrane-bound surface of the S4S5 linker, and we show that two highly conserved tyrosine residues within the KCNH subfamily of channels are membrane-associated. Site-directed mutagenesis and electrophysiological analysis indicates that Tyr-542 interacts with both the pore domain and voltage sensor residues to stabilize activated conformations of the channel, whereas Tyr-545 contributes to the slow kinetics of deactivation by primarily stabilizing the transition state between the activated and closed states. Thus, the two tyrosine residues in the Kv11.1 S4S5 linker play critical but distinct roles in the slow deactivation phenotype, which is a hallmark of Kv11.1 channels.

Indexed as

AnimalsCell MembraneERG1 Potassium ChannelFemaleHumansIon Channel GatingNuclear Magnetic Resonance, BiomolecularPeptidesXenopusERG1 Potassium ChannelKCNH2 protein, humanPeptideselectrophysiologygatinghERGion channelKv11.1lipid membranenuclear magnetic resonance (NMR)potassium channelS4S5 linkersite-directed mutagenesis

Identifiers

PMID27317659
PMCPMC5016128

What OpenQuestion holds

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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.