Evidence map›Paper›PMID 31672538›Full record

ReviewBiochimica et biophysica acta. Biomembranes2020

Disruption of palmitate-mediated localization; a shared pathway of force and anesthetic activation of TREK-1 channels.

E Nicholas Petersen, Mahmud Arif Pavel, Hao Wang, Scott B Hansen

Open access · greenAbstract readReview
In one paragraph

Review in Biochimica et biophysica acta. Biomembranes, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.6field-weighted citation impact, top 16% 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

17 citing papers in PubMed, 35 citations in OpenAlex.

  1. The short (and messy) life of the protagon theory of anaesthesia.History and philosophy of the life sciences · 2026
    Article
  2. Article
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  7. Review
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  13. Regulation of beta-amyloid production in neurons by astrocyte-derived cholesterol.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  14. The role of high cholesterol in age-related COVID19 lethality.bioRxiv : the preprint server for biology · 2021
    Article
  15. Hydroxychloroquine: mechanism of action inhibiting SARS-CoV2 entry.bioRxiv : the preprint server for biology · 2020
    Article
  16. Roles of Membrane Domains in Integrin-Mediated Cell Adhesion.International journal of molecular sciences · 2020
    Review
  17. Studies on the mechanism of general anesthesia.Proceedings of the National Academy of Sciences of the United States of America · 2020
    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 at 1 institution in 1 country.

E Nicholas PetersenDepartment of Molecular Medicine, The Scripps Research Institute, Jupiter, FL 33458, USA; Department of Neuroscience, The Scripps Research Institute, Jupiter, FL 33458, USA.
Mahmud Arif PavelDepartment of Molecular Medicine, The Scripps Research Institute, Jupiter, FL 33458, USA; Department of Neuroscience, The Scripps Research Institute, Jupiter, FL 33458, USA.
Hao WangDepartment of Molecular Medicine, The Scripps Research Institute, Jupiter, FL 33458, USA; Department of Neuroscience, The Scripps Research Institute, Jupiter, FL 33458, USA.
Scott B HansenDepartment of Molecular Medicine, 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
The role of lipid raft disruption in the activation of TREK-1 channels by anestheticsR01NS112534 · NINDS · UNIVERSITY OF FLORIDA · PI HANSEN, SCOTT B · 2019 to 2023
$2.2M
NINDS NIH HHS DP2 NS087943NINDS NIH HHS R01 NS112534
6 · The paper itself

Abstract

TWIK related K+ channel (TREK-1) is a mechano- and anesthetic sensitive channel that when activated attenuates pain and causes anesthesia. Recently the enzyme phospholipase D2 (PLD2) was shown to bind to the channel and generate a local high concentration of phosphatidic acid (PA), an anionic signaling lipid that gates TREK-1. In a biological membrane, the cell harnesses lipid heterogeneity (lipid compartments) to control gating of TREK-1 using palmitate-mediated localization of PLD2. Here we discuss the ability of mechanical force and anesthetics to disrupt palmitate-mediated localization of PLD2 giving rise to TREK-1's mechano- and anesthetic-sensitive properties. The likely consequences of this indirect lipid-based mechanism of activation are discussed in terms of a putative model for excitatory and inhibitory mechano-effectors and anesthetic sensitive ion channels in a biological context. Lastly, we discuss the ability of locally generated PA to reach mM concentrations near TREK-1 and the biophysics of localized signaling. Palmitate-mediated localization of PLD2 emerges as a central control mechanism of TREK-1 responding to mechanical force and anesthetic action. This article is part of a Special Issue entitled: Molecular biophysics of membranes and membrane proteins.

Indexed as

AnestheticsAnimalsHumansIon Channel GatingMechanical PhenomenaPalmitatesPhospholipase DPotassium Channels, Tandem Pore DomainAnestheticsPalmitatesPhospholipase Dphospholipase D2potassium channel protein TREK-1Potassium Channels, Tandem Pore DomainAnesthesiaLipidMechanosensationPalmitoylationRaftsSuper resolution microscopy

Identifiers

PMID31672538
PMCPMC6907892
OpenAlexW2982294226

What OpenQuestion holds

Textmetadata
LicenceTDM
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.