Evidence map›Paper›PMID 23884414›Full record

ArticleThe Journal of biological chemistry2013

Extracellular zinc ion regulates transient receptor potential melastatin 5 (TRPM5) channel activation through its interaction with a pore loop domain.

Kunitoshi Uchida, Makoto Tominaga

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing 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

14 citing papers in PubMed.

  1. Review
  2. Article
  3. TRPM3, TRPM4, and TRPM5 as thermo-sensitive channels.The journal of physiological sciences : JPS · 2024
    Review
  4. Review
  5. Article
  6. Review
  7. Article
  8. TRPM4 and TRPM5 Channels Share Crucial Amino Acid Residues for CaInternational journal of molecular sciences · 2019
    Article
  9. TRPM7, Magnesium, and Signaling.International journal of molecular sciences · 2019
    Review
  10. Selective inhibitory effects of zinc on cell proliferation in esophageal squamous cell carcinoma through Orai1.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2018
    Article
  11. Impact of Labile Zinc on Heart Function: From Physiology to Pathophysiology.International journal of molecular sciences · 2017
    Review
  12. Zinc transporters and dysregulated channels in cancers.Frontiers in bioscience (Landmark edition) · 2017
    Review
  13. Review
  14. 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

2 authors.

Kunitoshi UchidaFrom the Division of Cell Signaling, National Institute for Physiological Sciences (Okazaki Institutes for Integrative Bioscience), National Institutes of Natural Sciences, Okazaki 444-8787, Japan and; the Department of Physiological Sciences, The Graduate University for Advanced Studies, Okazaki 444-8585, Japan. Electronic address: kuchida@nips.ac.jp.
Makoto TominagaFrom the Division of Cell Signaling, National Institute for Physiological Sciences (Okazaki Institutes for Integrative Bioscience), National Institutes of Natural Sciences, Okazaki 444-8787, Japan and; the Department of Physiological Sciences, The Graduate University for Advanced Studies, Okazaki 444-8585, Japan. Electronic address: kuchida@nips.ac.jp.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The transient receptor potential melastatin 5 (TRPM5) channel is a monovalent cation channel activated by intracellular Ca(2+). Expression of this channel is restricted to taste cells, the pancreas and brainstem, and is thought to be involved in controlling membrane potentials. Its endogenous ligands are not well characterized. Here, we show that extracellular application of Zn(2+) inhibits TRPM5 activity. In whole-cell patch-clamp recordings, extracellular application of ZnCl2 inhibited step-pulse-induced TRPM5 currents with 500 nM free intracellular Ca(2+) in a dose-dependent manner (IC50 = 4.3 μM at -80 mV). ZnSO4 also inhibited TRPM5 activity. Extracellular application of ZnCl2 inhibited TRPM5 activation at several temperatures. Furthermore, inhibition by 30 μM ZnCl2 was impaired in TRPM5 mutants in which His at 896, and Glu at 926 and/or Glu at 939 in the outer pore loop were replaced with Gln. From these results, we conclude that extracellular Zn(2+) inhibits TRPM5 channels, and the residues in the outer pore loop of TRPM5 are critically involved in the inhibition.

Indexed as

Amino Acid SubstitutionCations, DivalentChloridesHEK293 CellsHumansMembrane PotentialsMouthwashesMutation, MissenseProtein Structure, SecondaryProtein Structure, TertiaryTRPM Cation ChannelsZincZinc CompoundsCations, DivalentChloridesMouthwashesTRPM5 protein, humanTRPM Cation ChannelsZinczinc chlorideZinc CompoundsCalciumIon ChannelsPatch Clamp ElectrophysiologyTRP ChannelsZinc

Identifiers

PMID23884414
PMCPMC3764799

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.