Evidence map›Paper›PMID 27291418›Full record

ArticleScientific reports2016

A molecular determinant of phosphoinositide affinity in mammalian TRPV channels.

Phanindra Velisetty, Istvan Borbiro, Marina A Kasimova, Luyu Liu, Doreen Badheka, Vincenzo Carnevale, Tibor Rohacs

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.6field-weighted citation impact, top 12% 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

16 citing papers in PubMed, 27 citations in OpenAlex.

  1. Bidirectional Allosteric Coupling between PIPInternational journal of molecular sciences · 2024
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  12. The Journal of neuroscience : the official journal of the Society for Neuroscience · 2019
    Article
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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

7 authors at 3 institutions in 1 country.

Phanindra VelisettyDepartment of Pharmacology, Physiology and Neuroscience, Rutgers - New Jersey Medical School, Newark, NJ 07103, USA.
Istvan BorbiroDepartment of Pharmacology, Physiology and Neuroscience, Rutgers - New Jersey Medical School, Newark, NJ 07103, USA.
Marina A KasimovaInstitute for Computational Molecular Science at Temple University in Philadelphia, PA, 19122, USA.
Luyu LiuDepartment of Pharmacology, Physiology and Neuroscience, Rutgers - New Jersey Medical School, Newark, NJ 07103, USA.
Doreen BadhekaDepartment of Pharmacology, Physiology and Neuroscience, Rutgers - New Jersey Medical School, Newark, NJ 07103, USA.
Vincenzo CarnevaleInstitute for Computational Molecular Science at Temple University in Philadelphia, PA, 19122, USA.
Tibor RohacsDepartment of Pharmacology, Physiology and Neuroscience, Rutgers - New Jersey Medical School, Newark, NJ 07103, USA.
Rutgers New Jersey Medical SchoolRutgers, The State University of New Jersey · USTemple University · US

Funding

X-ray and Neutron Interferometry Studies of Anesthetic Interactions with VoltageP01GM055876 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI LOLL, PATRICK J · 1997 to 2017
$22.4M
Regulation of sensory TRP channels by phospholipids and G-proteinsR01NS055159 · NINDS · UNIV OF MED/DENT OF NJ-NJ MEDICAL SCHOOL · PI ROHACS, TIBOR · 2007 to 2022
$5.9M
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
NIGMS NIH HHS P01 GM055876NIGMS NIH HHS R01 GM093290NINDS NIH HHS R01 NS055159
6 · The paper itself

Abstract

Phosphatidylinositol 4,5-bisphosphate [PI(4,5)P2] is an important cofactor for ion channels. Affinity for this lipid is a major determinant of channel inhibition by depletion of PI(4,5)P2 upon phospholipase C (PLC) activation. Little is known about what determines PI(4,5)P2 affinity in mammalian ion channels. Here we report that two members of the Transient Receptor Potential Vanilloid (TRPV) ion channel family, TRPV5 and TRPV6 lack a positively charged residue in the TM4-TM5 loop that was shown to interact with PI(4,5)P2 in TRPV1, which shows high affinity for this lipid. When this positively charged residue was introduced to either TRPV6 or TRPV5, they displayed markedly higher affinities for PI(4,5)P2, and were largely resistant to inhibition by PI(4,5)P2 depletion. Furthermore, Ca(2+)-induced inactivation of TRPV6 was essentially eliminated in the G488R mutant, showing the importance of PLC-mediated PI(4,5)P2 depletion in this process. Computational modeling shows that the introduced positive charge interacts with PI(4,5)P2 in TRPV6.

Indexed as

AnimalsCalciumCalcium ChannelsCiona intestinalisComputer SimulationHEK293 CellsHumansLipidsMolecular ConformationMolecular Docking SimulationMutationOocytesPatch-Clamp TechniquesPhosphatidylinositolsPhospholipasesProtein BindingCalciumCalcium ChannelsLipidsPhosphatidylinositolsPhospholipasesTRPV1 protein, humanTRPV5 protein, humanTRPV6 protein, humanTRPV Cation Channels

Identifiers

PMID27291418
PMCPMC4904367
OpenAlexW2441603154

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.