Evidence map›Paper›PMID 27628598›Full record

ArticleScientific reports2016

The coiled-coil domain of zebrafish TRPM7 regulates Mg·nucleotide sensitivity.

Chad Jansen, Jaya Sahni, Sayuri Suzuki, F David Horgen, Reinhold Penner, Andrea Fleig

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 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
3.0field-weighted citation impact, top 10% 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

12 citing papers in PubMed, 21 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Structural mechanism of TRPM7 channel regulation by intracellular magnesium.Cellular and molecular life sciences : CMLS · 2022
    Article
  5. Review
  6. Contribution of Coiled-Coil Assembly to CaJournal of the American Society of Nephrology : JASN · 2019
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. 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 1 country.

Chad JansenCenter for Biomedical Research, The Queen's Medical Center and University of Hawaii, Honolulu, HI-96813, USA.
Jaya SahniCenter for Immunity and Immunotherapies, Seattle Children's Research Institute, 1900 9th Ave, Seattle, WA 98101, USA.
Sayuri SuzukiCenter for Biomedical Research, The Queen's Medical Center and University of Hawaii, Honolulu, HI-96813, USA.
F David HorgenLaboratory of Marine Biological Chemistry, Department of Natural Sciences, Hawaii Pacific University, Kaneohe, HI 96744, USA.
Reinhold PennerCenter for Biomedical Research, The Queen's Medical Center and University of Hawaii, Honolulu, HI-96813, USA.
Andrea FleigCenter for Biomedical Research, The Queen's Medical Center and University of Hawaii, Honolulu, HI-96813, USA.
Hawaii Pacific University · USQueen's Medical Center · USUniversity of Hawaiʻi at Mānoa · USUniversity of Hawaii Cancer CenterUniversity of Hawaii System · US

Funding

UH Hilo COP A&RP20GM103466 · NIGMS · UNIVERSITY OF HAWAII AT MANOA · PI Youping Deng · 2012 to 2026
$60.3M
Regulation of Metal Ion Homeostasis by Channel KinasesP01GM078195 · NIGMS · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI RYAZANOV, ALEXEY G. · 2007 to 2011
$8.7M
NIGMS NIH HHS P01 GM078195NIGMS NIH HHS P20 GM103466
6 · The paper itself

Abstract

TRPM7 is a member of the Transient-Receptor-Potential Melastatin ion channel family. TRPM7 is a unique fusion protein of an ion channel and an α-kinase. Although mammalian TRPM7 is well characterized biophysically and its pivotal role in cancer, ischemia and cardiovascular disease is becoming increasingly evident, the study of TRPM7 in mouse models has been hampered by embryonic lethality of transgenic ablations. In zebrafish, functional loss of TRPM7 (drTRPM7) manifests itself in an array of non-lethal physiological malfunctions. Here, we investigate the regulation of wild type drTRPM7 and multiple C-terminal truncation mutants. We find that the biophysical properties of drTRPM7 are very similar to mammalian TRPM7. However, pharmacological profiling reveals that drTRPM7 is facilitated rather than inhibited by 2-APB, and that the TRPM7 inhibitor waixenicin A has no effect. This is reminiscent of the pharmacological profile of human TRPM6, the sister channel kinase of TRPM7. Furthermore, using truncation mutations, we show that the coiled-coil domain of drTRPM7 is involved in the channel's regulation by magnesium (Mg) and Mg·adenosine triphosphate (Mg·ATP). We propose that drTRPM7 has two protein domains that regulate inhibition by intracellular magnesium and nucleotides, and one domain that is concerned with sensing magnesium only.

Indexed as

Adenosine TriphosphateAnimalsBiophysical PhenomenaBoron CompoundsCell ProliferationChickensElectric ConductivityHEK293 CellsHumansHydrogen-Ion ConcentrationLiverMagnesiumMutant ProteinsOsmolar ConcentrationProtein DomainsProtein Serine-Threonine Kinases2-aminoethyl diphenylborinateAdenosine TriphosphateBoron CompoundsMagnesiumMutant ProteinsProtein Serine-Threonine KinasesTrpm7 protein, zebrafishTRPM Cation ChannelsZebrafish Proteins

Identifiers

PMID27628598
PMCPMC5024298
OpenAlexW2519621022

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

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.