Evidence map›Paper›PMID 29556099›Full record

ArticleNature chemical biology2018

An optically controlled probe identifies lipid-gating fenestrations within the TRPC3 channel.

Michaela Lichtenegger, Oleksandra Tiapko, Barbora Svobodova, Thomas Stockner, Toma N Glasnov, Wolfgang Schreibmayer, Dieter Platzer, Gema Guedes de la Cruz, Sarah Krenn, Romana Schober and 4 more

Abstract read
In one paragraph

Article in Nature chemical biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers.

0numbers the graph read from it
0cells of the map it votes in
75citing papers in PubMed
5.2field-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

75 citing papers in PubMed, 120 citations in OpenAlex.

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  10. Impact of C-Terminal PKC Phosphorylation on TRPC6 Current Kinetics.International journal of molecular sciences · 2025
    Article
  11. Review
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  14. Synthetic Lipid Biology.Chemical reviews · 2025
    Review
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  17. Article
  18. Article
  19. Thermosensing ability of TRPC5: current knowledge and unsettled questions.The journal of physiological sciences : JPS · 2024
    Review
  20. Review

15 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

14 authors at 4 institutions in 1 country.

Michaela LichteneggerGottfried Schatz Research Center, Biophysics, Medical University of Graz, Graz, Austria.
Oleksandra TiapkoGottfried Schatz Research Center, Biophysics, Medical University of Graz, Graz, Austria.
Barbora SvobodovaGottfried Schatz Research Center, Biophysics, Medical University of Graz, Graz, Austria.
Thomas StocknerInstitute of Pharmacology, Medical University of Vienna, Vienna, Austria.
Toma N GlasnovInstitute of Chemistry, University of Graz, Graz, Austria.
Wolfgang SchreibmayerGottfried Schatz Research Center, Biophysics, Medical University of Graz, Graz, Austria.
Dieter PlatzerGottfried Schatz Research Center, Biophysics, Medical University of Graz, Graz, Austria.
Gema Guedes de la CruzInstitute of Chemistry, University of Graz, Graz, Austria.
Sarah KrennGottfried Schatz Research Center, Biophysics, Medical University of Graz, Graz, Austria.
Romana SchoberInstitute of Biophysics, University of Linz, Linz, Austria.
Niroj ShresthaGottfried Schatz Research Center, Biophysics, Medical University of Graz, Graz, Austria.
Rainer SchindlGottfried Schatz Research Center, Biophysics, Medical University of Graz, Graz, Austria.ORCID 0000-0003-0896-8887
Christoph RomaninInstitute of Biophysics, University of Linz, Linz, Austria.ORCID 0000-0003-3756-4136
Klaus GroschnerGottfried Schatz Research Center, Biophysics, Medical University of Graz, Graz, Austria. klaus.groschner@medunigraz.at.ORCID 0000-0002-8659-377X
Medical University of Graz · ATJohannes Kepler University of Linz · ATUniversity of Graz · ATMedical University of Vienna · AT

Funding

Austrian Science Fund FWF P 26067Austrian Science Fund FWF P 27263Austrian Science Fund FWF P 28701Austrian Science Fund FWF W 1226
6 · The paper itself

Abstract

Transient receptor potential canonical (TRPC) channels TRPC3, TRPC6 and TRPC7 are able to sense the lipid messenger diacylglycerol (DAG). The DAG-sensing and lipid-gating processes in these ion channels are still unknown. To gain insights into the lipid-sensing principle, we generated a DAG photoswitch, OptoDArG, that enabled efficient control of TRPC3 by light. A structure-guided mutagenesis screen of the TRPC3 pore domain unveiled a single glycine residue behind the selectivity filter (G652) that is exposed to lipid through a subunit-joining fenestration. Exchange of G652 with larger residues altered the ability of TRPC3 to discriminate between different DAG molecules. Light-controlled activation-deactivation cycling of TRPC3 channels by an OptoDArG-mediated optical 'lipid clamp' identified pore domain fenestrations as pivotal elements of the channel´s lipid-sensing machinery. We provide evidence for a novel concept of lipid sensing by TRPC channels based on a lateral fenestration in the pore domain that accommodates lipid mediators to control gating.

Indexed as

Ion Channel GatingAnimalsCalciumGlycineHEK293 CellsHumansKineticsLightLipidsMutagenesisMutationOptics and PhotonicsPhotochemistryProtein BindingRatsSignal TransductionCalciumGlycineLipidsTRPC3 cation channelTRPC Cation ChannelsTrpv1 protein, ratTRPV Cation Channels

Identifiers

PMID29556099
PMCPMC5903546
OpenAlexW2791305882

What OpenQuestion holds

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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.