Evidence map›Paper›PMID 30644819›Full record

ArticleeLife2019

Conserved allosteric pathways for activation of TRPV3 revealed through engineering vanilloid-sensitivity.

Feng Zhang, Kenton Jon Swartz, Andres Jara-Oseguera

Open access · goldAbstract read
In one paragraph

Article in eLife, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed, 1 pooled it
3.0field-weighted citation impact, top 10% 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

21 citing papers in PubMed, 1 synthesis or guideline pooled it, 36 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Cannabidiol sensitizes TRPV2 channels to activation by 2-APB.bioRxiv : the preprint server for biology · 2023
    Article
  9. Article
  10. Structural Pharmacology of TRP Channels.Journal of molecular biology · 2021
    Review
  11. Mapping temperature-dependent conformational change in the voltage-sensing domain of an engineered heat-activated KProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  12. Review
  13. Article
  14. Gating of human TRPV3 in a lipid bilayer.Nature structural & molecular biology · 2020
    Article
  15. Review
  16. Review
  17. Review
  18. Article
  19. Article
  20. 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

3 authors at 1 institution in 1 country.

Feng ZhangMolecular Physiology and Biophysics Section, Porter Neuroscience Research Center, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, United States.
Kenton Jon SwartzMolecular Physiology and Biophysics Section, Porter Neuroscience Research Center, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, United States.ORCID 0000-0003-3419-0765
Andres Jara-OsegueraMolecular Physiology and Biophysics Section, Porter Neuroscience Research Center, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, United States.ORCID 0000-0001-5921-9320
National Institutes of Health · US

Funding

Gating mechanisms and pharmacology of voltage-activated ion channelsZIANS002945 · NINDS · NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE · PI SWARTZ, KENTON · 2009 to 2025
$44.2M
NINDS NIH HHS Intramural Research Program NS002945NINDS NIH HHS K99 Pathway to Independence Award
6 · The paper itself

Abstract

The Transient Receptor Potential Vanilloid 1 (TRPV) channel is activated by an array of stimuli, including heat and vanilloid compounds. The TRPV1 homologues TRPV2 and TRPV3 are also activated by heat, but sensitivity to vanilloids and many other agonists is not conserved among TRPV subfamily members. It was recently discovered that four mutations in TRPV2 are sufficient to render the channel sensitive to the TRPV1-specific vanilloid agonist resiniferatoxin (RTx). Here, we show that mutation of six residues in TRPV3 corresponding to the vanilloid site in TRPV1 is sufficient to engineer RTx binding. However, robust activation of TRPV3 by RTx requires facilitation of channel opening by introducing mutations in the pore, temperatures > 30°C, or sensitization with another agonist. Our results demonstrate that the energetics of channel activation can determine the apparent sensitivity to a stimulus and suggest that allosteric pathways for activation are conserved in the TRPV family.

Indexed as

Protein EngineeringAllosteric RegulationAmino Acid SequenceAnimalsBinding SitesDiterpenesMiceMutationProtein DomainsRatsTemperatureTRPV Cation ChannelsDiterpenesresiniferatoxinTrpv3 protein, mouseTRPV Cation Channelsion channel gatingmolecular biophysicsmouseneuroscienceratresiniferaroxinstructural biologyTRP channelTRPVvanilloidxenopus

Identifiers

PMID30644819
PMCPMC6333442
OpenAlexW2895963202

What OpenQuestion holds

Textmetadata
LicenceCC0
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.