ArticleCellular signalling2011
The channel-kinase TRPM7 regulates phosphorylation of the translational factor eEF2 via eEF2-k.
Article in Cellular signalling, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers, 1 of them a synthesis that pooled it.
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Who cites it
46 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Serum Magnesium Levels in Preterm Infants Are Higher Than Adult Levels: A Systematic Literature Review and Meta-Analysis.Nutrients · 2017Pooled it
- TRPM7 kinase: a target for multimodal drug development in neurological disorders.Acta pharmacologica Sinica · 2026Review
- Physiological functions and pharmacological targeting of transient receptor potential channels.Pharmacological reviews · 2025Review
- MgScience advances · 2025Article
- Unlocking TRPM7 interactions: A database-driven quest.Computational and structural biotechnology journal · 2025Review
- TRPM channels in health and disease.Nature reviews. Nephrology · 2024Review
- Pathophysiological Roles of Transient Receptor Potential (Trp) Channels and Zinc Toxicity in Brain Disease.International journal of molecular sciences · 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
- The molecular appearance of native TRPM7 channel complexes identified by high-resolution proteomics.eLife · 2021Article
- Potential Implications of Mammalian Transient Receptor Potential Melastatin 7 in the Pathophysiology of Myalgic Encephalomyelitis/Chronic Fatigue Syndrome: A Review.International journal of environmental research and public health · 2021Review
- TRPM7 is critical for short-term synaptic depression by regulating synaptic vesicle endocytosis.eLife · 2021Article
- Magnesium Deficiency Causes a Reversible, Metabolic, Diastolic Cardiomyopathy.Journal of the American Heart Association · 2021Article
- Phagocytic activity of splenic macrophages is enhanced and accompanied by cytosolic alkalinization in TRPM7 kinase-dead mice.The FEBS journal · 2021Article
- Mapping TRPM7 Function by NS8593.International journal of molecular sciences · 2020Review
- Genetic variants in TRPM7 associated with unexplained stillbirth modify ion channel function.Human molecular genetics · 2020Article
- Inhibition of TRPM7 blocks MRTF/SRF-dependent transcriptional and tumorigenic activity.Oncogene · 2020Article
- TRPM7 Induces Tumorigenesis and Stemness Through Notch Activation in Glioma.Frontiers in pharmacology · 2020Article
- Role of the chanzyme TRPM7 in the nervous system in health and disease.Cellular and molecular life sciences : CMLS · 2019Review
- Solution Structure of the Carboxy-Terminal Tandem Repeat Domain of Eukaryotic Elongation Factor 2 Kinase and Its Role in Substrate Recognition.Journal of molecular biology · 2019Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Protein translation is an essential but energetically expensive process, which is carefully regulated in accordance to the cellular nutritional and energy status. Eukaryotic elongation factor 2 (eEF2) is a central regulation point since it mediates ribosomal translocation and can be inhibited by phosphorylation at Thr56. TRPM7 is the unique fusion of an ion channel with a functional Ser/Thr-kinase. While TRPM7's channel function has been implicated in regulating vertebrate Mg(2+) uptake required for cell growth, the function of its kinase domain remains unclear. Here, we show that under conditions where cell growth is limited by Mg(2+) availability, TRPM7 via its kinase mediates enhanced Thr56 phosphorylation of eEF2. TRPM7-kinase does not appear to directly phosphorylate eEF2, but rather to influence the amount of eEF2's cognate kinase eEF2-k, involving its phosphorylation at Ser77. These findings suggest that TRPM7's structural duality ensures ideal positioning of its kinase in close proximity to channel-mediated Mg(2+) uptake, allowing for the adjustment of protein translational rates to the availability of Mg(2+).
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