Evidence map›Paper›PMID 21624095›Full record

ReviewActa physiologica (Oxford, England)2012

Integration of transient receptor potential canonical channels with lipids.

D J Beech

Open access · bronzeAbstract readReview
In one paragraph

Review in Acta physiologica (Oxford, England), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

30 citing papers in PubMed, 60 citations in OpenAlex.

  1. Trial
  2. Article
  3. Lipid Regulation of Mechanosensitive Ion Channels.International journal of molecular sciences · 2026
    Review
  4. Article
  5. Functional characterization of the αFrontiers in pharmacology · 2025
    Article
  6. Review
  7. Article
  8. Review
  9. Contribution of TRPC3-mediated CaPflugers Archiv : European journal of physiology · 2023
    Article
  10. Article
  11. Review
  12. How TRPC Channels Modulate Hippocampal Function.International journal of molecular sciences · 2020
    Review
  13. Review
  14. Article
  15. Review
  16. Review
  17. Review
  18. Review
  19. Article
  20. 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

1 author at 1 institution in 1 country.

D J BeechFaculty of Biological Sciences, Institute of Membrane and Systems Biology, University of Leeds, UK. d.j.beech@leeds.ac.uk
University of Leeds · GB

Funding

Wellcome Trust 083857
6 · The paper itself

Abstract

Transient receptor potential canonical (TRPC) channels are the canonical (C) subset of the TRP proteins, which are widely expressed in mammalian cells. They are thought to be primarily involved in determining calcium and sodium entry and have wide-ranging functions that include regulation of cell proliferation, motility and contraction. The channels are modulated by a multiplicity of factors, putatively existing as integrators in the plasma membrane. This review considers the sensitivities of TRPC channels to lipids that include diacylglycerols, phosphatidylinositol bisphosphate, lysophospholipids, oxidized phospholipids, arachidonic acid and its metabolites, sphingosine-1-phosphate, cholesterol and some steroidal derivatives and other lipid factors such as gangliosides. Promiscuous and selective lipid sensing have been detected. There appear to be close working relationships with lipids of the phospholipase C and A(2) enzyme systems, which may enable integration with receptor signalling and membrane stretch. There are differences in the properties of each TRPC channel that are further complicated by TRPC heteromultimerization. The lipids modulate activity of the channels or insertion in the plasma membrane. Lipid microenvironments and intermediate sensing proteins have been described that include caveolae, G protein signalling, SEC14-like and spectrin-type domains 1 (SESTD1) and podocin. The data suggest that lipid sensing is an important aspect of TRPC channel biology enabling integration with other signalling systems.

Indexed as

AnimalsArachidonic AcidCalciumCholesterolHumansLysophospholipidsMembrane LipidsMicePhospholipidsSignal TransductionSphingosineTRPC Cation ChannelsArachidonic AcidCalciumCholesterolLysophospholipidsMembrane LipidsPhospholipidsSphingosinesphingosine 1-phosphateTRPC Cation Channels

Identifiers

PMID21624095
PMCPMC3734623
OpenAlexW2119827013

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.