Evidence map›Paper›PMID 24855944›Full record

ArticleCell2014

The TRPM7 chanzyme is cleaved to release a chromatin-modifying kinase.

Grigory Krapivinsky, Luba Krapivinsky, Yunona Manasian, David E Clapham

Open access · bronzeAbstract read
In one paragraph

Article in Cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 117 papers.

0numbers the graph read from it
0cells of the map it votes in
117citing papers in PubMed
10.7field-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

117 citing papers in PubMed, 178 citations in OpenAlex.

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  12. Sudden Death-AssociatedbioRxiv : the preprint server for biology · 2025
    Article
  13. Article
  14. MgScience advances · 2025
    Article
  15. Article
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  18. Article
  19. Article
  20. Unlocking TRPM7 interactions: A database-driven quest.Computational and structural biotechnology journal · 2025
    Review

57 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 1 country.

Grigory KrapivinskyHoward Hughes Medical Institute, Department of Cardiology, Boston Children's Hospital, Enders Building 1309, 320 Longwood Avenue, Boston, MA 02115, USA.
Luba KrapivinskyHoward Hughes Medical Institute, Department of Cardiology, Boston Children's Hospital, Enders Building 1309, 320 Longwood Avenue, Boston, MA 02115, USA.
Yunona ManasianHoward Hughes Medical Institute, Department of Cardiology, Boston Children's Hospital, Enders Building 1309, 320 Longwood Avenue, Boston, MA 02115, USA.
David E ClaphamHoward Hughes Medical Institute, Department of Cardiology, Boston Children's Hospital, Enders Building 1309, 320 Longwood Avenue, Boston, MA 02115, USA; Department of Neurobiology, Harvard Medical School, 220 Longwood Avenue, Boston, MA 02115, USA. Electronic address: dclapham@enders.tch.harvard.edu.
Boston Children's Hospital · USHoward Hughes Medical Institute · US

Funding

SYNAPTIC MECHANISMS IN HIPPOCAMPAL EPILEPTOGENESISP30HD018655 · NICHD · CHILDREN'S HOSPITAL BOSTON · PI POMEROY, SCOTT LOREN · 1985 to 2015
$26.2M
Howard Hughes Medical InstituteNICHD NIH HHS P30 HD018655
6 · The paper itself

Abstract

TRPM7 is a ubiquitous ion channel and kinase, a unique "chanzyme," required for proper early embryonic development. It conducts Zn(2+), Mg(2+), and Ca(2+) as well as monovalent cations and contains a functional serine/threonine kinase at its carboxyl terminus. Here, we show that in normal tissues and cell lines, the kinase is proteolytically cleaved from the channel domain in a cell-type-specific manner. These TRPM7 cleaved kinase fragments (M7CKs) translocate to the nucleus and bind multiple components of chromatin-remodeling complexes, including Polycomb group proteins. In the nucleus, the kinase phosphorylates specific serines/threonines of histones. M7CK-dependent phosphorylation of H3Ser10 at promoters of TRPM7-dependent genes correlates with their activity. We also demonstrate that cytosolic free [Zn(2+)] is TRPM7 dependent and regulates M7CK binding to transcription factors containing zinc-finger domains. These findings suggest that TRPM7-mediated modulation of intracellular Zn(2+) concentration couples ion-channel signaling to epigenetic chromatin covalent modifications that affect gene expression patterns. PAPERCLIP:

Indexed as

AnimalsCell LineCell NucleusChromatin Assembly and DisassemblyCytosolGene ExpressionHistonesHumansMicePhosphorylationProtein Serine-Threonine KinasesTRPM Cation ChannelsZincZinc FingersHistonesProtein Serine-Threonine KinasesTRPM7 protein, humanTrpm7 protein, mouseTRPM Cation ChannelsZinc

Identifiers

PMID24855944
PMCPMC4156102
OpenAlexW2078712719

What OpenQuestion holds

Textmetadata
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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.