Evidence map›Paper›PMID 17217066›Full record

ReviewHandbook of experimental pharmacology2007

The Mg2+ and Mg(2+)-nucleotide-regulated channel-kinase TRPM7.

R Penner, A Fleig

Abstract readReview
In one paragraph

Review in Handbook of experimental pharmacology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
20.2field-weighted citation impact, top 1% 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

44 citing papers in PubMed, 95 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. The Role of TRPM7 in Oncogenesis.International journal of molecular sciences · 2024
    Review
  5. Ischemia-Reperfusion Increases TRPM7 Expression in Mouse Retinas.International journal of molecular sciences · 2023
    Article
  6. Review
  7. Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Functional expression of TRPM7 as a CaPhysiological reports · 2019
    Article
  14. Role of TRPM7 in cerebral ischaemia and hypoxia.The Journal of physiology · 2017
    Review
  15. Article
  16. Article
  17. ESC heart failure · 2016
    Article
  18. Article
  19. Review
  20. 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 at 1 institution in 1 country.

R PennerLaboratory of Cell and Molecular Signaling, The Queen's Medical Center, 1301 Punchbowl Street-UHT 8, Honolulu, HI 96813, USA.
A Fleig
Queen's Medical Center · US

Funding

CALCIUM SIGNALING ACTIVATION PROCESS OF MICROGLIA CELLSR01NS040927 · NINDS · QUEEN'S MEDICAL CENTER · PI PENNER, REINHOLD · 2001 to 2005
$1.8M
Magnesium-nucleotide depletion activated ion channelR01GM065360 · NIGMS · QUEEN'S MEDICAL CENTER · PI FLEIG, ANDREA · 2002 to 2005
$1.1M
NIGMS NIH HHS R01 GM065360NIGMS NIH HHS R01-GM065360NINDS NIH HHS R01 NS040927NINDS NIH HHS R01-NS040927
6 · The paper itself

Abstract

TRPM7 is a member of the melastatin-related subfamily of TRP channels and represents a protein that contains both an ion channel and a kinase domain. The protein is ubiquitously expressed and represents the only ion channel known that is essential for cellular viability. TRPM7 is a divalent cation-selective ion channel that is permeable to Ca2+ and Mg2+, but also conducts essential metals such as Zn2+, Mn2+, and Co2+, as well as nonphysiologic or toxic metals such as Ni2+, Cd2+, Ba2+, and Sr2+. The channel is constitutively open but strongly downregulated by intracellular levels of Mg2+ and MgATP and other Mg-nucleotides. Reducing the cellular levels of these regulators leads to activation of TRPM7-mediated currents that exhibit a characteristic nonlinear current-voltage relationship with pronounced outward rectification due to divalent influx at physiologically negative voltages and monovalent outward fluxes at positive voltages. TRPM7 channel activity is also actively regulated following receptor-mediated changes in cyclic AMP (cAMP) and protein kinase A activity. This regulation as well as that by Mg-nucleotides requires a functional endogenous kinase domain. The function of the kinase domain is not completely understood, but may involve autophosphorylation of TRPM7 as well as phosphorylation of other target proteins such as annexin and myosin IIA heavy chain. Based on these properties, TRPM7 is currently believed to represent a ubiquitous homeostatic mechanism that regulates Ca2+ and Mg2+ fluxes based on the metabolic state of the cell. Physiologically, the channel may serve as a regulated transport mechanism for these ions that could affect cell adhesion, cell growth and proliferation, and even cell death under pathological stress such as anoxia.

Indexed as

Adenosine TriphosphateAnimalsBiotransformationGene Expression RegulationHumansIon ChannelsMagnesiumPhosphotransferasesProtein Serine-Threonine KinasesTRPM Cation ChannelsAdenosine TriphosphateIon ChannelsMagnesiumPhosphotransferasesProtein Serine-Threonine KinasesTRPM7 protein, humanTrpm7 protein, mouseTrpm7 protein, ratTRPM Cation Channels

Identifiers

PMID17217066
PMCPMC5663631
OpenAlexW2126276276

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.