Evidence map›Paper›PMID 19940139›Full record

ArticleThe Journal of biological chemistry2010

Constitutive activity of the human TRPML2 channel induces cell degeneration.

Shaya Lev, David A Zeevi, Ayala Frumkin, Vered Offen-Glasner, Gideon Bach, Baruch Minke

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
3.2field-weighted citation impact, top 9% 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

28 citing papers in PubMed, 56 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. A Seven-Gene Signature with Close Immune Correlation Was Identified for Survival Prediction of Lung Adenocarcinoma.Medical science monitor : international medical journal of experimental and clinical research · 2020
    Article
  14. Endolysosomal CaCancers · 2018
    Review
  15. Article
  16. Article
  17. Review
  18. Novel Role of TRPML2 in the Regulation of the Innate Immune Response.Journal of immunology (Baltimore, Md. : 1950) · 2015
    Article
  19. Review
  20. Ion channels in cancer: future perspectives and clinical potential.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2014
    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 1 institution in 1 country.

Shaya LevDepartment of Medical Neurobiology and the Kühne Minerva Center for Studies of Visual Transduction, Faculty of Medicine of the Hebrew University, Jerusalem, Israel.
David A Zeevi
Ayala Frumkin
Vered Offen-Glasner
Gideon Bach
Baruch Minke
Hebrew University of Jerusalem · IL

Funding

GENETIC DISSECTION OF PHOTOTRANSDUCTIONR01EY003529 · NEI · HEBREW UNIVERSITY OF JERUSALEM · PI MINKE, BARUCH · 1985 to 2011
$1.8M
NEI NIH HHS R01 EY003529NEI NIH HHS R01 EY 03529
6 · The paper itself

Abstract

The mucolipin (TRPML) ion channel proteins represent a distinct subfamily of channel proteins within the transient receptor potential (TRP) superfamily of cation channels. Mucolipin 1, 2, and 3 (TRPML1, -2, and -3, respectively) are channel proteins that share high sequence homology with each other and homology in the transmembrane domain with other TRPs. Mutations in the TRPML1 protein are implicated in mucolipidosis type IV, whereas mutations in TRPML3 are found in the varitint-waddler mouse. The properties of the wild type TRPML2 channel are not well known. Here we show functional expression of the wild type human TRPML2 channel (h-TRPML2). The channel is functional at the plasma membrane and characterized by a significant inward rectification similar to other constitutively active TRPML mutant isoforms. The h-TRPML2 channel displays nonselective cation permeability, which is Ca(2+)-permeable and inhibited by low extracytosolic pH but not Ca(2+) regulated. In addition, constitutively active h-TRPML2 leads to cell death by causing Ca(2+) overload. Furthermore, we demonstrate by functional mutation analysis that h-TRPML2 shares similar characteristics and structural similarities with other TRPML channels that regulate the channel in a similar manner. Hence, in addition to overall structure, all three TRPML channels also share common modes of regulation.

Indexed as

AnimalsApoptosisCalciumCationsCell MembraneDrosophilaGene ExpressionHeLa CellsHumansHydrogen-Ion ConcentrationKidneyMembrane PotentialsMicePatch-Clamp TechniquesPlasma Membrane Calcium-Transporting ATPasesPoint MutationCalciumCationsMcoln2 protein, humanMCOLN3 protein, humanPlasma Membrane Calcium-Transporting ATPasesTransient Receptor Potential Channels

Identifiers

PMID19940139
PMCPMC2807332
OpenAlexW2031561272

What OpenQuestion holds

Textmetadata
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.