Evidence map›Paper›PMID 25633344›Full record

ReviewBiochimica et biophysica acta2015

Lipid agonism: The PIP2 paradigm of ligand-gated ion channels.

Scott B Hansen

Open access · hybridAbstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 85 papers.

0numbers the graph read from it
0cells of the map it votes in
85citing papers in PubMed
5.7field-weighted citation impact, top 3% 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

85 citing papers in PubMed, 149 citations in OpenAlex.

  1. Article
  2. Hydrophobic mismatch induces lipid sorting based on tail unsaturation.bioRxiv : the preprint server for biology · 2026
    Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Lipid probes to study ion channels.Current opinion in chemical biology · 2025
    Review
  9. Activation of Smooth Muscle KInternational journal of molecular sciences · 2025
    Article
  10. Review
  11. The plasma membrane inner leaflet PI(4,5)PNature communications · 2024
    Article
  12. Article
  13. Article
  14. Cooperative Gating of a KJournal of the American Chemical Society · 2024
    Article
  15. Review
  16. Article
  17. The mechanism ofProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  18. Article
  19. Functional Regulation of Aquaporin Dynamics by Lipid Bilayer Composition.bioRxiv : the preprint server for biology · 2023
    Article
  20. Article

25 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

1 author at 1 institution in 1 country.

Scott B HansenDepartment of Molecular Therapeutics, The Scripps Research Institute, Jupiter FL 33458, USA; Department of Neuroscience, The Scripps Research Institute, Jupiter FL 33458, USA. Electronic address: shansen@scripps.edu.
Scripps Research Institute · US

Funding

Molecular Mechanism of MechanosensationDP2NS087943 · NINDS · SCRIPPS FLORIDA · PI HANSEN, SCOTT B · 2013 to 2013
$2.8M
NCCDPHP CDC HHS 1DP2NS087943-01NINDS NIH HHS DP2 NS087943
6 · The paper itself

Abstract

The past decade, membrane signaling lipids emerged as major regulators of ion channel function. However, the molecular nature of lipid binding to ion channels remained poorly described due to a lack of structural information and assays to quantify and measure lipid binding in a membrane. How does a lipid-ligand bind to a membrane protein in the plasma membrane, and what does it mean for a lipid to activate or regulate an ion channel? How does lipid binding compare to activation by soluble neurotransmitter? And how does the cell control lipid agonism? This review focuses on lipids and their interactions with membrane proteins, in particular, ion channels. I discuss the intersection of membrane lipid biology and ion channel biophysics. A picture emerges of membrane lipids as bona fide agonists of ligand-gated ion channels. These freely diffusing signals reside in the plasma membrane, bind to the transmembrane domain of protein, and cause a conformational change that allosterically gates an ion channel. The system employs a catalog of diverse signaling lipids ultimately controlled by lipid enzymes and raft localization. I draw upon pharmacology, recent protein structure, and electrophysiological data to understand lipid regulation and define inward rectifying potassium channels (Kir) as a new class of PIP2 lipid-gated ion channels.

Indexed as

Ion Channel GatingAnimalsHumansLigand-Gated Ion ChannelsLigandsMembrane MicrodomainsMembrane PotentialsModels, MolecularPhosphatidylinositol 4,5-DiphosphatePotassium Channels, Inwardly RectifyingProtein ConformationStructure-Activity RelationshipLigand-Gated Ion ChannelsLigandsPhosphatidylinositol 4,5-DiphosphatePotassium Channels, Inwardly RectifyingG-proteinIon channelLipid gatedLipid raftPIP(2)Signaling lipid

Identifiers

PMID25633344
PMCPMC4540326
OpenAlexW2013853780

What OpenQuestion holds

Textmetadata
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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.