Evidence map›Paper›PMID 26469389›Full record

ArticleScientific reports2015

Migration of PIP2 lipids on voltage-gated potassium channel surface influences channel deactivation.

Liping Chen, Qiansen Zhang, Yunguang Qiu, Zanyuan Li, Zhuxi Chen, Hualiang Jiang, Yang Li, Huaiyu Yang

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.8field-weighted citation impact, top 14% 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

27 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. Review
  3. Bidirectional Allosteric Coupling between PIPInternational journal of molecular sciences · 2024
    Article
  4. Functional Characterization of a Spectrum of Novel Romano-Ward SyndromeInternational journal of molecular sciences · 2023
    Article
  5. Clinically RelevantInternational journal of molecular sciences · 2022
    Article
  6. Review
  7. Article
  8. Tracking Membrane Protein Dynamics in Real Time.The Journal of membrane biology · 2021
    Review
  9. Review
  10. Review
  11. Modulation of KFrontiers in pharmacology · 2020
    Article
  12. TwoFrontiers in physiology · 2020
    Article
  13. Article
  14. Review
  15. Review
  16. Article
  17. Science advances · 2019
    Article
  18. Article
  19. Review
  20. Article
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

8 authors at 2 institutions in 1 country.

Liping ChenState Key Laboratory of Drug Research and Key Laboratory of Receptor Research, Shanghai Institute of Materia Medical, Chinese Academy of Sciences, Shanghai, 201203, China.
Qiansen ZhangState Key Laboratory of Drug Research and Key Laboratory of Receptor Research, Shanghai Institute of Materia Medical, Chinese Academy of Sciences, Shanghai, 201203, China.
Yunguang QiuState Key Laboratory of Drug Research and Key Laboratory of Receptor Research, Shanghai Institute of Materia Medical, Chinese Academy of Sciences, Shanghai, 201203, China.
Zanyuan LiState Key Laboratory of Drug Research and Key Laboratory of Receptor Research, Shanghai Institute of Materia Medical, Chinese Academy of Sciences, Shanghai, 201203, China.
Zhuxi ChenState Key Laboratory of Drug Research and Key Laboratory of Receptor Research, Shanghai Institute of Materia Medical, Chinese Academy of Sciences, Shanghai, 201203, China.
Hualiang JiangState Key Laboratory of Drug Research and Key Laboratory of Receptor Research, Shanghai Institute of Materia Medical, Chinese Academy of Sciences, Shanghai, 201203, China.
Yang LiState Key Laboratory of Drug Research and Key Laboratory of Receptor Research, Shanghai Institute of Materia Medical, Chinese Academy of Sciences, Shanghai, 201203, China.
Huaiyu YangState Key Laboratory of Drug Research and Key Laboratory of Receptor Research, Shanghai Institute of Materia Medical, Chinese Academy of Sciences, Shanghai, 201203, China.
Chinese Academy of Sciences · CNShanghai Institute of Materia Medica · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Published studies of lipid-protein interactions have mainly focused on lipid binding to an individual site of the protein. Here, we show that a lipid can migrate between different binding sites in a protein and this migration modulates protein function. Voltage-gated potassium (Kv) channels have several potential binding sites for phosphatidylinositol-4,5-bisphosphate (PIP2). Our molecular dynamics (MD) simulations on the KCNQ2 channel reveal that PIP2 preferentially binds to the S4-S5 linker when the channel is in the open state while maintains a certain probability of migrating to the S2-S3 linker. Guided by the MD results, electrophysiological experiments using KCNQ2, KCNQ1, and hERG channels show that the migration of PIP2 toward the S2-S3 linker controls the deactivation rate of the channel. The data suggest that PIP2 can migrate between different binding sites in Kv channels with significant impacts on channel deactivation, casting new insights into the dynamics and physiological functions of lipid-protein interactions.

Indexed as

AnimalsCHO CellsCricetulusEther-A-Go-Go Potassium ChannelsHumansKCNQ2 Potassium ChannelModels, MolecularMolecular ConformationMolecular Dynamics SimulationMutationPhosphatidylinositol 4,5-DiphosphatePotassium Channels, Voltage-GatedProtein BindingStructure-Activity RelationshipEther-A-Go-Go Potassium ChannelsKCNQ2 Potassium ChannelPhosphatidylinositol 4,5-DiphosphatePotassium Channels, Voltage-Gated

Identifiers

PMID26469389
PMCPMC4606798
OpenAlexW2417477273

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.