Evidence map›Paper›PMID 35686986›Full record

ArticleeLife2022

Sequence and structural conservation reveal fingerprint residues in TRP channels.

Deny Cabezas-Bratesco, Francisco A Mcgee, Charlotte K Colenso, Kattina Zavala, Daniele Granata, Vincenzo Carnevale, Juan C Opazo, Sebastian E Brauchi

Abstract read
In one paragraph

Article in eLife, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
–field-weighted citation impact
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

17 citing papers in PubMed.

  1. Article
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  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. The odyssey of the TR(i)P journey to the cellular membrane.Frontiers in cell and developmental biology · 2024
    Review
  14. Article
  15. Article
  16. Progress in the Structural Basis of thermoTRP Channel Polymodal Gating.International journal of molecular sciences · 2023
    Review
  17. 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

8 authors.

Deny Cabezas-Bratesco *Instituto de Fisiologia, Facultad de Medicina, Universidad Austral de Chile, Valdivia, Chile.
Francisco A Mcgee *Institute for Computational Molecular Science and Department of Biology, Temple University, Philadelphia, United States.
Charlotte K ColensoInstituto de Fisiologia, Facultad de Medicina, Universidad Austral de Chile, Valdivia, Chile.
Kattina ZavalaInstituto de Ciencias Ambientales y Evolutivas, Facultad de Ciencias, Universidad Austral de Chile, Valdivia, Chile.
Daniele GranataInstitute for Computational Molecular Science and Department of Biology, Temple University, Philadelphia, United States.
Vincenzo CarnevaleInstitute for Computational Molecular Science and Department of Biology, Temple University, Philadelphia, United States.ORCID 0000-0002-1918-8280
Juan C OpazoInstituto de Ciencias Ambientales y Evolutivas, Facultad de Ciencias, Universidad Austral de Chile, Valdivia, Chile.ORCID 0000-0001-7938-4083
Sebastian E BrauchiInstituto de Fisiologia, Facultad de Medicina, Universidad Austral de Chile, Valdivia, Chile.ORCID 0000-0002-8494-9912

Funding

Regulation of the Intestinal Ca2+ Channels TRPV6R01GM093290 · NIGMS · UNIV OF MED/DENT OF NJ-NJ MEDICAL SCHOOL · PI CARNEVALE, VINCENZO, ROHACS, TIBOR · 2011 to 2025
$4.9M
Molecular mechanism of TRPV1 activationR01GM131048 · NIGMS · TEMPLE UNIV OF THE COMMONWEALTH · PI CARNEVALE, VINCENZO, ROHACS, TIBOR · 2019 to 2022
$1.4M
Computer Cluster for Computational Biology and BiophysicsS10OD020095 · OD · TEMPLE UNIV OF THE COMMONWEALTH · PI LEVY, RONALD · 2015 to 2015
$442k
NIGMS NIH HHS R01 GM093290NIGMS NIH HHS R01 GM131048NIH HHS S10 OD020095
6 · The paper itself

Abstract

Transient receptor potential (TRP) proteins are a large family of cation-selective channels, surpassed in variety only by voltage-gated potassium channels. Detailed molecular mechanisms governing how membrane voltage, ligand binding, or temperature can induce conformational changes promoting the open state in TRP channels are still a matter of debate. Aiming to unveil distinctive structural features common to the transmembrane domains within the TRP family, we performed phylogenetic reconstruction, sequence statistics, and structural analysis over a large set of TRP channel genes. Here, we report an exceptionally conserved set of residues. This fingerprint is composed of twelve residues localized at equivalent three-dimensional positions in TRP channels from the different subtypes. Moreover, these amino acids are arranged in three groups, connected by a set of aromatics located at the core of the transmembrane structure. We hypothesize that differences in the connectivity between these different groups of residues harbor the apparent differences in coupling strategies used by TRP subgroups.

Indexed as

Transient Receptor Potential ChannelsPhylogenyProtein DomainsTransient Receptor Potential Channelsallosterismevolutionevolutionary biologyMSAstructureTRP channels

Identifiers

PMID35686986
PMCPMC9242649

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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.