Evidence map›Paper›PMID 21262820›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2011

Optical probing of a dynamic membrane interaction that regulates the TREK1 channel.

Guillaume Sandoz, Sarah C Bell, Ehud Y Isacoff

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
2.9field-weighted citation impact, top 8% 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

31 citing papers in PubMed, 62 citations in OpenAlex.

  1. TREK2 Lipid Binding Preferences Revealed by Native Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2024
    Article
  2. Article
  3. Review
  4. Article
  5. PIPInternational journal of molecular sciences · 2020
    Article
  6. Review
  7. Ion Channels and Thermosensitivity: TRP, TREK, or Both?International journal of molecular sciences · 2019
    Review
  8. Article
  9. Article
  10. Article
  11. Cardiovascular pharmacology of KNaunyn-Schmiedeberg's archives of pharmacology · 2018
    Article
  12. Article
  13. Identification of critical amino acids in the proximal C-terminal of TREK-2 KPflugers Archiv : European journal of physiology · 2018
    Article
  14. Article
  15. Article
  16. Article
  17. Heterodimerization within the TREK channel subfamily produces a diverse family of highly regulated potassium channels.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  18. Article
  19. Article
  20. Much more than a leak: structure and function of K₂p-channels.Pflugers Archiv : European journal of physiology · 2015
    Review
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

3 authors at 3 institutions in 2 countries.

Guillaume SandozDepartment of Molecular and Cell Biology, Helen Wills Neuroscience Institute, University of California, Berkeley, CA 94720, USA.
Sarah C Bell
Ehud Y Isacoff
Lawrence Berkeley National Laboratory · USUniversity of California, Berkeley · USUniversity of California, San Francisco · US

Funding

STRUCTURAL REARRANGEMENTS IN CHANNEL GATINGR01NS035549 · NINDS · UNIVERSITY OF CALIFORNIA BERKELEY · PI ISACOFF, EHUD · 1996 to 2013
$4.1M
NINDS NIH HHS R01 NS035549NINDS NIH HHS R01 NS35549
6 · The paper itself

Abstract

TREK channels produce background currents that regulate cell excitability. These channels are sensitive to a wide variety of stimuli including polyunsaturated fatty acids (PUFAs), phospholipids, mechanical stretch, and intracellular acidification. They are inhibited by neurotransmitters, hormones, and pharmacological agents such as the antidepressant fluoxetine. TREK1 knockout mice have impaired PUFA-mediated neuroprotection to ischemia, reduced sensitivity to volatile anesthetics, altered perception of pain, and a depression-resistant phenotype. Here, we investigate TREK1 regulation by Gq-coupled receptors (GqPCR) and phospholipids. Several reports indicate that the C-terminal domain of TREK1 is a key regulatory domain. We developed a fluorescent-based technique that monitors the plasma membrane association of the C terminus of TREK1 in real time. Our fluorescence and functional experiments link the modulation of TREK1 channel function by internal pH, phospholipid, and GqPCRs to TREK1-C-terminal domain association to the plasma membrane, where increased association results in greater activity. In keeping with this relation, inhibition of TREK1 current by fluoxetine is found to be accompanied by dissociation of the C-terminal domain from the membrane.

Indexed as

AnimalsAntidepressive Agents, Second-GenerationCell MembraneFatty Acids, UnsaturatedFluoxetineHEK293 CellsHumansHydrogen-Ion ConcentrationIschemiaMiceMice, KnockoutMicroscopy, FluorescenceOocytesPhospholipidsPotassium Channels, Tandem Pore DomainProtein Structure, TertiaryAntidepressive Agents, Second-GenerationFatty Acids, UnsaturatedFluoxetinePhospholipidspotassium channel protein TREK-1Potassium Channels, Tandem Pore Domain

Identifiers

PMID21262820
PMCPMC3038738
OpenAlexW2135122106

What OpenQuestion holds

Textmetadata
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.