ArticleScientific reports2017
Mass Spectrometric Analysis of TRPM6 and TRPM7 Phosphorylation Reveals Regulatory Mechanisms of the Channel-Kinases.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
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Who cites it
20 citing papers in PubMed, 31 citations in OpenAlex.
- The PACT Network: PRL, ARL, CNNM, and TRPM Proteins in Magnesium Transport and Disease.International journal of molecular sciences · 2025Review
- Functions of TRPs in retinal tissue in physiological and pathological conditions.Frontiers in molecular neuroscience · 2024Review
- Effect of truncation on TRPM7 channel activity.Channels (Austin, Tex.) · 2023Article
- Essential role of MgCell reports · 2023Article
- TRP Channels in Tumoral Processes Mediated by Oxidative Stress and Inflammation.Antioxidants (Basel, Switzerland) · 2023Review
- Cardiovascular toxicity of tyrosine kinase inhibitors during cancer treatment: Potential involvement of TRPM7.Frontiers in cardiovascular medicine · 2023Review
- On the modulation of TRPM channels: Current perspectives and anticancer therapeutic implications.Frontiers in oncology · 2022Review
- CNNM proteins selectively bind to the TRPM7 channel to stimulate divalent cation entry into cells.PLoS biology · 2021Article
- The molecular appearance of native TRPM7 channel complexes identified by high-resolution proteomics.eLife · 2021Article
- Mapping TRPM7 Function by NS8593.International journal of molecular sciences · 2020Review
- Structure of the AAVhu.37 capsid by cryoelectron microscopy.Acta crystallographica. Section F, Structural biology communications · 2020Article
- Investigating Phosphorylation Patterns of the Ion Channel TRPM7 Using Multiple Extraction and Enrichment Techniques Reveals New Phosphosites.Journal of the American Society for Mass Spectrometry · 2019Article
- TRPM7, Magnesium, and Signaling.International journal of molecular sciences · 2019Review
- O-GlcNAcylation of PERIOD regulates its interaction with CLOCK and timing of circadian transcriptional repression.PLoS genetics · 2019Article
- TRPM7 residue S1269 mediates cAMP dependence of Ca2+ influx.PloS one · 2019Article
- Depletion of plasma membrane-associated phosphoinositides mimics inhibition of TRPM7 channels by cytosolic MgThe Journal of biological chemistry · 2018Article
- Review
- The kinase activity of the channel-kinase protein TRPM7 regulates stability and localization of the TRPM7 channel in polarized epithelial cells.The Journal of biological chemistry · 2018Article
- Histone phosphorylation by TRPM6's cleaved kinase attenuates adjacent arginine methylation to regulate gene expression.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Different Principles of ADP-Ribose-Mediated Activation and Opposite Roles of the NUDT9 Homology Domain in the TRPM2 Orthologs of Man and Sea Anemone.Frontiers in physiology · 2017Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
TRPM7 and TRPM6 were the first identified bifunctional channels to contain their own kinase domains, but how these channel-kinases are regulated is poorly understood. Previous studies identified numerous phosphorylation sites on TRPM7, but very little is known about TRPM6 phosphorylation or sites on TRPM7 transphosphorylated by TRPM6. Our mass spectrometric analysis of homomeric and heteromeric TRPM7 and TRPM6 channels identified phosphorylation sites on both proteins, as well as several prominent sites on TRPM7 that are commonly modified through autophosphorylation and transphosphorylation by TRPM6. We conducted a series of amino acid substitution analyses and identified S1777, in TRPM7's catalytic domain, and S1565, in TRPM7's exchange domain that mediates kinase dimerization, as potential regulatory sites. The phosphomimetic S1777D substitution disrupted catalytic activity, most likely by causing an electrostatic perturbation at the active site. The S1565D phosphomimetic substitution also inactivated the kinase but did so without interfering with kinase dimerization. Molecular modeling indicates that phosphorylation of S1565 is predicted to structurally affect TRPM7's functionally conserved N/D loop, which is thought to influence the access of substrate to the active site pocket. We propose that phosphorylation of S1565 within the exchange domain functions as a regulatory switch to control TRPM7 catalytic activity.
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Registered trials
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.