Evidence map›Paper›PMID 24827085›Full record

ArticleScientific reports2014

Differential modulations of KCNQ1 by auxiliary proteins KCNE1 and KCNE2.

Pan Li, Haowen Liu, Chaohua Lai, Peibei Sun, Wenping Zeng, Fangming Wu, Longhua Zhang, Sheng Wang, Changlin Tian, Jiuping Ding

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2014. 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
0.8field-weighted citation impact, top 25% 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, 18 citations in OpenAlex.

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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

10 authors at 3 institutions in 1 country.

Pan Li1] Hefei National Laboratory for Physical Science at Microscale and School of Life Science, University of Science and Technology of China, Hefei, Anhui, 230027, P. R. China [2].
Haowen Liu1] Key laboratory of Molecular Biophysics of the Ministry of Education College of Life Science and Technology, Huazhong University of Science and Technology, Wuhan, Hubei, 430074, P, R. China [2].
Chaohua LaiHefei National Laboratory for Physical Science at Microscale and School of Life Science, University of Science and Technology of China, Hefei, Anhui, 230027, P. R. China.
Peibei SunHefei National Laboratory for Physical Science at Microscale and School of Life Science, University of Science and Technology of China, Hefei, Anhui, 230027, P. R. China.
Wenping ZengKey laboratory of Molecular Biophysics of the Ministry of Education College of Life Science and Technology, Huazhong University of Science and Technology, Wuhan, Hubei, 430074, P, R. China.
Fangming WuHigh Magnetic Field Laboratory, Chinese Academy of Sciences, Hefei, Anhui, 230031, P. R. China.
Longhua ZhangHefei National Laboratory for Physical Science at Microscale and School of Life Science, University of Science and Technology of China, Hefei, Anhui, 230027, P. R. China.
Sheng WangKey laboratory of Molecular Biophysics of the Ministry of Education College of Life Science and Technology, Huazhong University of Science and Technology, Wuhan, Hubei, 430074, P, R. China.
Changlin Tian1] Hefei National Laboratory for Physical Science at Microscale and School of Life Science, University of Science and Technology of China, Hefei, Anhui, 230027, P. R. China [2] High Magnetic Field Laboratory, Chinese Academy of Sciences, Hefei, Anhui, 230031, P. R. China.
Jiuping DingKey laboratory of Molecular Biophysics of the Ministry of Education College of Life Science and Technology, Huazhong University of Science and Technology, Wuhan, Hubei, 430074, P, R. China.
Huazhong University of Science and Technology · CNUniversity of Science and Technology of China · CNHigh Magnetic Field Laboratory · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

KCNQ1 channels play vital roles in cardiovascular, gastric and other systems. The conductance and dynamics of KCNQ1 could be modulated by different single transmembrane helical auxiliary proteins (such as KCNE1, KCNE2 and others). In this study, detail KCNQ1 function modulations by different regions of KCNE1 or KCNE2 were examined using combinational methods of electrophysiology, immunofluorescence, solution NMR and related backbone flexibility analysis. In the presence of KCNE2 N-terminus, decreased surface expression and consequent low activities of KCNQ1 were observed. The transmembrane domains (TMDs) of KCNE1 and KCNE2 were illustrated to associate with the KCNQ1 channel in different modes: Ile64 in KCNE2-TMD interacting with Phe340 and Phe275 in KCNQ1, while two pairs of interacting residues (Phe340-Thr58 and Ala244-Tyr65) in the KCNQ1/KCNE1 complex. The KCNE1 C-terminus could modulate gating property of KCNQ1, whereas KCNE2 C-terminus had only minimal influences on KCNQ1. All of the results demonstrated different KCNQ1 function modulations by different regions of the two auxiliary proteins.

Indexed as

Cell LineHEK293 CellsHumansKCNQ1 Potassium ChannelMembrane ProteinsMicellesPotassium Channels, Voltage-GatedProtein Interaction Domains and MotifsProtein Structure, TertiaryKCNE1 protein, humanKCNE2 protein, humanKCNQ1 Potassium ChannelKCNQ1 protein, humanMembrane ProteinsMicellesPotassium Channels, Voltage-Gated

Identifiers

PMID24827085
PMCPMC4021338
OpenAlexW2040481055

What OpenQuestion holds

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LicenceCC BY-NC-SA
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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.