Evidence map›Paper›PMID 27162025›Full record

ArticleFASEB journal : official publication of the Federation of American Societies for Experimental Biology2016

Novel exon 1 protein-coding regions N-terminally extend human KCNE3 and KCNE4.

Geoffrey W Abbott

Open access · bronzeAbstract read
In one paragraph

Article in FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.6field-weighted citation impact, top 15% 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

12 citing papers in PubMed, 16 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Review
  5. Kv7 Channels and Excitability Disorders.Handbook of experimental pharmacology · 2021
    Article
  6. Article
  7. Article
  8. Targeted deletion ofFASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2017
    Article
  9. Article
  10. Article
  11. Article
  12. Review
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

1 author at 1 institution in 1 country.

Geoffrey W AbbottBioelectricity Laboratory, Department of Pharmacology and Department of Physiology and Biophysics, School of Medicine, University of California, Irvine, Irvine, California, USA abbottg@uci.edu.
University of California, Irvine · US

Funding

THYROID SODIUM I/ SYMPORTERR01DK041544 · NIDDK · YESHIVA UNIVERSITY · PI ABBOTT, GEOFFREY W, CARRASCO, NANCY · 1989 to 2017
$5.6M
Ion channel-transporter interactionsR01GM115189 · NIGMS · UNIVERSITY OF CALIFORNIA-IRVINE · PI ABBOTT, GEOFFREY W · 2015 to 2018
$1.1M
NIDDK NIH HHS R01 DK041544NIGMS NIH HHS R01 GM115189
6 · The paper itself

Abstract

The 5 human (h)KCNE β subunits each regulate various cation channels and are linked to inherited cardiac arrhythmias. Reported here are previously undiscovered protein-coding regions in exon 1 of hKCNE3 and hKCNE4 that extend their encoded extracellular domains by 44 and 51 residues, which yields full-length proteins of 147 and 221 residues, respectively. Full-length hKCNE3 and hKCNE4 transcript and protein are expressed in multiple human tissues; for hKCNE4, only the longer protein isoform is detectable. Two-electrode voltage-clamp electrophysiology revealed that, when coexpressed in Xenopus laevis oocytes with various potassium channels, the newly discovered segment preserved conversion of KCNQ1 by hKCNE3 to a constitutively open channel, but prevented its inhibition of Kv4.2 and KCNQ4. hKCNE4 slowing of Kv4.2 inactivation and positive-shifted steady-state inactivation were also preserved in the longer form. In contrast, full-length hKCNE4 inhibition of KCNQ1 was limited to 40% at +40 mV vs. 80% inhibition by the shorter form, and augmentation of KCNQ4 activity by hKCNE4 was entirely abolished by the additional segment. Among the genome databases analyzed, the longer KCNE3 is confined to primates; full-length KCNE4 is widespread in vertebrates but is notably absent from Mus musculus Findings highlight unexpected KCNE gene diversity, raise the possibility of dynamic regulation of KCNE partner modulation via splice variation, and suggest that the longer hKCNE3 and hKCNE4 proteins should be adopted in future mechanistic and genetic screening studies.-Abbott, G. W. Novel exon 1 protein-coding regions N-terminally extend human KCNE3 and KCNE4.

Indexed as

Amino Acid SequenceAnimalsGene Expression RegulationHumansOocytesPatch-Clamp TechniquesPotassium Channels, Voltage-GatedProtein ConformationProtein Processing, Post-TranslationalXenopus laevisKCNE3 protein, humanKCNE4 protein, humanPotassium Channels, Voltage-GatedarrhythmiaKCNQ1KCNQ4Kv4.2potassium channel

Identifiers

PMID27162025
PMCPMC6137956
OpenAlexW2392632094

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.