Evidence map›Paper›PMID 29196683›Full record

ArticleScientific reports2017

Preferential selection of Arginine at the lipid-water-interface of TRPV1 during vertebrate evolution correlates with its snorkeling behaviour and cholesterol interaction.

Somdatta Saha, Arijit Ghosh, Nikhil Tiwari, Ashutosh Kumar, Abhishek Kumar, Chandan Goswami

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

18 citing papers in PubMed, 36 citations in OpenAlex.

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  7. Progress in the Structural Basis of thermoTRP Channel Polymodal Gating.International journal of molecular sciences · 2023
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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

6 authors at 1 institution in 2 countries.

Somdatta SahaSchool of Biological Sciences, National Institute of Science Education and Research, Institute of Physics Campus, Bhubaneswar, 751005, Orissa, India.
Arijit GhoshSchool of Biological Sciences, National Institute of Science Education and Research, Institute of Physics Campus, Bhubaneswar, 751005, Orissa, India.
Nikhil TiwariSchool of Biological Sciences, National Institute of Science Education and Research, Institute of Physics Campus, Bhubaneswar, 751005, Orissa, India.
Ashutosh KumarSchool of Biological Sciences, National Institute of Science Education and Research, Institute of Physics Campus, Bhubaneswar, 751005, Orissa, India.
Abhishek KumarMolecular Genetic Epidemiology, Deutsches Krebsforschungszentrum (DKFZ), Heidelberg, Germany.ORCID 0000-0003-4172-4059
Chandan GoswamiSchool of Biological Sciences, National Institute of Science Education and Research, Institute of Physics Campus, Bhubaneswar, 751005, Orissa, India. chandan@niser.ac.in.
National Institute of Science Education and Research · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

TRPV1 is a thermo-sensitive ion channel involved in neurosensory and other physiological functions. The trans-membrane helices of TRPV1 undergo quick and complex conformational changes governed by thermodynamic parameters and membrane components leading to channel opening. However, the molecular mechanisms underlying such events are poorly understood. Here we analysed the molecular evolution of TRPV1 at the lipid-water-interface region (LWI), typically defined as a layer of 6 Å thickness on each side of the membrane with less availability of free water. Amino acids demarcating the end of the trans-membrane helices are highly conserved. Residues present in the inner leaflet are more conserved and have been preferentially selected over others. Amino acids with snorkeling properties (Arginine and Tyrosine) undergo specific selection during the vertebrate evolution in a cholesterol-dependent and/or body temperature manner. Results suggest that H-bond formation between the OH- group of cholesterol and side chain of Arg557 or Arg575 at the inner leaflet is a critical parameter that can regulate channel functions. Different LWI mutants of TRPV1 have altered membrane localization and deficient colocalization with lipid raft markers. These findings may help to understand the lipid-protein interactions, and molecular basis of different neuronal functions. Such findings may have broad importance in the context of differential sensory responses, pathophysiologies, and application of pharmacological drugs such as anaesthetics acting on TRPVs.

Indexed as

Amino Acid MotifsAnimalsArginineBehavior, AnimalBinding SitesBiological EvolutionCell LineCholesterolCryoelectron MicroscopyMembrane MicrodomainsModels, MolecularMolecular Docking SimulationMutagenesis, Site-DirectedProtein StabilityRatsThermodynamicsArginineCholesterolTrpv1 protein, ratTRPV Cation ChannelsWater

Identifiers

PMID29196683
PMCPMC5711878
OpenAlexW2770062712

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Registered trials

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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.