Evidence map›Paper›PMID 22760061›Full record

ArticleChannels (Austin, Tex.)

Voltage-sensing phosphatase reveals temporal regulation of TRPC3/C6/C7 channels by membrane phosphoinositides.

Kyohei Itsuki, Yuko Imai, Yasushi Okamura, Kihachiro Abe, Ryuji Inoue, Masayuki X Mori

Open access · goldAbstract read
In one paragraph

Article in Channels (Austin, Tex.). The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.9field-weighted citation impact, top 33% 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

11 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Article
  3. Engineering an enhanced voltage-sensing phosphatase.The Journal of general physiology · 2020
    Article
  4. Article
  5. Phosphatidylinositol 4,5-bisphosphate (PIPThe Journal of biological chemistry · 2018
    Article
  6. Article
  7. Article
  8. Phosphoinositide regulation of TRPV1 revisited.Pflugers Archiv : European journal of physiology · 2015
    Review
  9. Article
  10. Phosphoinositide regulation of TRP channels.Handbook of experimental pharmacology · 2014
    Review
  11. Review
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 5 institutions in 4 countries.

Kyohei ItsukiDepartment of Physiology, School of Medicine, Fukuoka University, Japan.
Yuko Imai
Yasushi Okamura
Kihachiro Abe
Ryuji Inoue
Masayuki X Mori
Kyushu University · JPFukuoka University · JPGraduate School USA · USIndiana University School of MedicineUniversity of Dental Medicine · MM

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

TRPC3/C6/C7 channels, a subgroup of classical/canonical TRP channels, are activated by diacylglycerol produced via activation of phospholipase C (PLC)-coupled receptors. Recognition of the physiological importance of these channels has been steadily growing, but the mechanism by which they are regulated remains largely unknown. We recently used a membrane-resident danio rerio voltage-sensing phosphatase (DrVSP) to study TRPC3/C6/C7 regulation and found that the channel activity was controlled by PtdIns(4,5)P(2)-DAG signaling in a self-limiting manner (Imai Y et al., the Journal of Physiology, 2012). In this addendum, we present the advantages of using DrVSP as a molecular tool to study PtdIns(4,5)P(2) regulation. DrVSP should be readily applicable for studying phosphoinositide metabolism-linked channel regulation as well as lipid dynamics. Furthermore, in comparison to other modes of self-limiting ion channel regulation, the regulation of TRPC3/C6/C7 channels seems highly susceptible to activation signal strength, which could potentially affect both open duration and the time to peak activation and inactivation. Dysfunction of such self-limiting regulation may contribute to the pathology of the cardiovascular system, gastrointestinal tract and brain, as these channels are broadly distributed and affected by numerous neurohormonal agonists.

Indexed as

AnimalsCell Line, TransformedCiona intestinalisDiglyceridesHumansIon Channel GatingMicePhosphatidylinositol 4,5-DiphosphatePhosphoinositide Phospholipase CPhosphoric Monoester HydrolasesSpecies SpecificityTRPC6 Cation ChannelTRPC Cation ChannelsZebrafish ProteinsDiglyceridesPhosphatidylinositol 4,5-DiphosphatePhosphoinositide Phospholipase CPhosphoric Monoester Hydrolasestpte protein, zebrafishTRPC3 cation channelTRPC6 Cation ChannelTRPC6 protein, humanTrpc7 protein, mouseTRPC Cation Channelsvoltage-sensor-containing phosphatase, Ciona intestinalisZebrafish Proteins

Identifiers

PMID22760061
PMCPMC3431592
OpenAlexW1990364126

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.