Evidence map›Paper›PMID 22824268›Full record

ArticleBiophysical journal2012

The molecular mechanism by which PIP(2) opens the intracellular G-loop gate of a Kir3.1 channel.

Xuan-Yu Meng, Hong-Xing Zhang, Diomedes E Logothetis, Meng Cui

Abstract read
In one paragraph

Article in Biophysical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing 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

47 citing papers in PubMed.

  1. Understanding Ion Channel Gating Mechanisms by Molecular Dynamics Simulations.Advances in experimental medicine and biology · 2026
    Review
  2. Coordination of bilayer properties by an inward-rectifier KJournal of structural biology: X · 2024
    Article
  3. Cooperative Gating of a KJournal of the American Chemical Society · 2024
    Article
  4. Article
  5. Review
  6. From Crosstalk to Synergism: The Combined Effect of Cholesterol and PI(4,5)PAdvances in experimental medicine and biology · 2023
    Review
  7. Article
  8. Article
  9. Article
  10. A molecular switch controls the impact of cholesterol on a Kir channel.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  11. Subtype-selective positive modulation of KBritish journal of pharmacology · 2022
    Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Conduction through a narrow inward-rectifier KThe Journal of general physiology · 2019
    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

4 authors.

Xuan-Yu MengDepartment of Physiology and Biophysics, Virginia Commonwealth University School of Medicine, Richmond, VA, USA.
Hong-Xing Zhang
Diomedes E Logothetis
Meng Cui

Funding

Structural Determinants of PIP2 RegulationR01HL059949 · NHLBI · VIRGINIA COMMONWEALTH UNIVERSITY · PI Leigh Daniel Plant · 1998 to 2026
$11.6M
Modulation of Kir Channel Function by PhosphorylationR01HL090882 · NHLBI · VIRGINIA COMMONWEALTH UNIVERSITY · PI LOGOTHETIS, DIOMEDES E. · 2009 to 2012
$1.5M
High Performance Computing Cluster for Biomedical Research at VCUS10RR027411 · NCRR · VIRGINIA COMMONWEALTH UNIVERSITY · PI CUI, MENG · 2010 to 2010
$417k
NCRR NIH HHS S10 RR027411NCRR NIH HHS S10RR027411NHLBI NIH HHS HL059949NHLBI NIH HHS HL090882NHLBI NIH HHS R01 HL059949NHLBI NIH HHS R01 HL090882
6 · The paper itself

Abstract

Inwardly rectifying potassium (Kir) channels are characterized by a long pore comprised of continuous transmembrane and cytosolic portions. A high-resolution structure of a Kir3.1 chimera revealed the presence of the cytosolic (G-loop) gate captured in the closed or open conformations. Here, we conducted molecular-dynamics simulations of these two channel states in the presence and absence of phosphatidylinositol bisphosphate (PIP(2)), a phospholipid that is known to gate Kir channels. Simulations of the closed state with PIP(2) revealed an intermediate state between the closed and open conformations involving direct transient interactions with PIP(2), as well as a network of transitional inter- and intrasubunit interactions. Key elements in the G-loop gating transition involved a PIP(2)-driven movement of the N-terminus and C-linker that removed constraining intermolecular interactions and led to CD-loop stabilization of the G-loop gate in the open state. To our knowledge, this is the first dynamic molecular view of PIP(2)-induced channel gating that is consistent with existing experimental data.

Indexed as

Ion Channel GatingModels, ChemicalModels, MolecularBinding SitesComputer SimulationG Protein-Coupled Inwardly-Rectifying Potassium ChannelsIntracellular SpacePhosphatidylinositol 4,5-DiphosphatePorosityProtein BindingProtein ConformationProtein Structure, TertiaryG Protein-Coupled Inwardly-Rectifying Potassium ChannelsPhosphatidylinositol 4,5-Diphosphate

Identifiers

PMID22824268
PMCPMC3341553

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.