Evidence map›Paper›PMID 29866880›Full record

ArticleThe Journal of biological chemistry2018

The kinase activity of the channel-kinase protein TRPM7 regulates stability and localization of the TRPM7 channel in polarized epithelial cells.

Na Cai, Liping Lou, Namariq Al-Saadi, Sandra Tetteh, Loren W Runnels

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

20 citing papers in PubMed, 24 citations in OpenAlex.

  1. Review
  2. Article
  3. Identification of 14-3-3 Proteins as Binding Partners of TRP Channels.Journal of chemical information and modeling · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. MgJournal of cellular physiology · 2025
    Article
  9. Review
  10. Article
  11. The odyssey of the TR(i)P journey to the cellular membrane.Frontiers in cell and developmental biology · 2024
    Review
  12. Article
  13. Intracellular CaFrontiers in physiology · 2023
    Review
  14. Article
  15. Review
  16. Article
  17. Review
  18. Article
  19. The Presence and Distribution of TRPM7 in the Canine Mammary Glands.Animals : an open access journal from MDPI · 2020
    Article
  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

5 authors at 1 institution in 2 countries.

Na CaiDepartment of Pharmacology, Rutgers Robert Wood Johnson Medical School, Piscataway, New Jersey 08854.
Liping LouDepartment of Pharmacology, Rutgers Robert Wood Johnson Medical School, Piscataway, New Jersey 08854.
Namariq Al-SaadiDepartment of Pharmacology, Rutgers Robert Wood Johnson Medical School, Piscataway, New Jersey 08854; University of Misan, Amarah 62001, Iraq.
Sandra TettehDepartment of Pharmacology, Rutgers Robert Wood Johnson Medical School, Piscataway, New Jersey 08854.
Loren W RunnelsDepartment of Pharmacology, Rutgers Robert Wood Johnson Medical School, Piscataway, New Jersey 08854. Electronic address: runnellw@rwjms.rutgers.edu.
Rutgers, The State University of New Jersey · US

Funding

Functional Analysis of the Bifunctional Ion Channel and Kinase TRPM7R01GM080753 · NIGMS · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI RUNNELS, LOREN W · 2007 to 2016
$3.0M
NIGMS NIH HHS R01 GM080753
6 · The paper itself

Abstract

The channel-kinase transient receptor potential melastatin 7 (TRPM7) is a bifunctional protein with ion channel and kinase domains. The kinase activity of TRPM7 has been linked to the regulation of a broad range of cellular activities, but little is understood as to how the channel itself is regulated by its own kinase activity. Here, using several mammalian cell lines expressing WT TRPM7 or kinase-inactive variants, we discovered that compared with the cells expressing WT TRPM7, cells in which TRPM7's kinase activity was inactivated had faster degradation, elevated ubiquitination, and increased intracellular retention of the channel. Mutational analysis of TRPM7 autophosphorylation sites further revealed a role for Ser-1360 of TRPM7 as a key residue mediating both TRPM7 stability and intracellular trafficking. Additional trafficking roles were uncovered for Ser-1403 and Ser-1567, whose phosphorylation by TRPM7's kinase activity mediated the interaction of the channel with the signaling protein 14-3-3θ. In summary, our results point to a critical role for TRPM7's kinase activity in regulating proteasome-mediated turnover of the TRPM7 channel and controlling its cellular localization in polarized epithelial cells. Overall, these findings improve our understanding of the significance of TRPM7's kinase activity for functional regulation of its channel activity.

Indexed as

14-3-3 ProteinsAnimalsCell PolarityEpithelial CellsHEK293 CellsHumansMicePhosphorylationProtein BindingProtein KinasesProtein StabilityProtein TransportTRPM Cation Channels14-3-3 ProteinsProtein KinasesTrpm7 protein, mouseTRPM Cation Channels14-3-3 proteinion channelphosphorylationprotein kinaseproteosome-mediated turnovertransient receptor potential cation channel subfamily M member 7transient receptor potential channels (TRP channels)TRPM7

Identifiers

PMID29866880
PMCPMC6065181
OpenAlexW2806207257

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.