Evidence map›Paper›PMID 21427721›Full record

ArticleNature communications2011

Lipid-dependent gating of a voltage-gated potassium channel.

Hui Zheng, Weiran Liu, Lingyan Y Anderson, Qiu-Xing Jiang

Open access · hybridAbstract read
In one paragraph

Article in Nature communications, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
4.7field-weighted citation impact, top 4% 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

63 citing papers in PubMed, 102 citations in OpenAlex.

  1. Review
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  10. Fluctuating hydrogen-bond network of the Hv1 ion channel.Computational and structural biotechnology journal · 2025
    Article
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  19. High-Resolution Structures of KHandbook of experimental pharmacology · 2021
    Article
  20. A PIPCommunications biology · 2020
    Article

3 more citing papers are in PubMed but not listed here.

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.

Hui ZhengDepartment of Cell Biology, University of Texas Southwestern Medical Center, Dallas, Texas 75390, USA.
Weiran Liu
Lingyan Y Anderson
Qiu-Xing Jiang
The University of Texas Southwestern Medical Center · USUniversity of Houston · US

Funding

Structural study of a Kv channel in different conformations in membranesR01GM093271 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI JIANG, QIU-XING · 2010 to 2013
$1.2M
Obtaining 3D structures with subnanogram macromoleculesR01GM088745 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI JIANG, QIU-XING · 2009 to 2012
$1.0M
NIGMS NIH HHS R01 GM088745NIGMS NIH HHS R01GM088745NIGMS NIH HHS R01 GM093271NIGMS NIH HHS R01GM093271
6 · The paper itself

Abstract

Recent studies hypothesized that phospholipids stabilize two voltage-sensing arginine residues of certain voltage-gated potassium channels in activated conformations. It remains unclear how lipids directly affect these channels. Here, by examining the conformations of the KvAP in different lipids, we showed that without voltage change, the voltage-sensor domains switched from the activated to the resting state when their surrounding lipids were changed from phospholipids to nonphospholipids. Such lipid-determined conformational change was coupled to the ion-conducting pore, suggesting that parallel to voltage gating, the channel is gated by its annular lipids. Our measurements recognized that the energetic cost of lipid-dependent gating approaches that of voltage gating, but kinetically it appears much slower. Our data support that a channel and its surrounding lipids together constitute a functional unit, and natural nonphospholipids such as cholesterol should exert strong effects on voltage-gated channels. Our first observation of lipid-dependent gating may have general implications to other membrane proteins.

Indexed as

AeropyrumArchaeal ProteinsArginineCysteineGene ExpressionIon Channel GatingKineticsMembranes, ArtificialModels, MolecularMolecular ConformationMutagenesis, Site-DirectedPhospholipidsPotassium Channels, Voltage-GatedProtein Structure, TertiaryRecombinant ProteinsArchaeal ProteinsArginineCysteineMembranes, ArtificialPhospholipidsPotassium Channels, Voltage-GatedRecombinant Proteins

Identifiers

PMID21427721
PMCPMC3072105
OpenAlexW2107872165

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.