Abstract
The channel kinases TRPM6 and TRPM7 are fusion proteins with an ion transport domain and an enzymatically active kinase domain. TRPM7 has been found in every mammalian tissue investigated to date. The two-in-one protein structure, the ubiquitous expression profile, and the protein's unique biophysical characteristics that enable divalent ion transport involve TRPM7 in a plethora of (patho)physiological processes. With its prominent role in cellular and systemic magnesium homeostasis, TRPM7 emerges as a key player in embryonic development, global ischemia, cardiovascular disease, and cancer.
Publication types
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Research Support, N.I.H., Extramural
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Review
MeSH terms
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Animals
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Cell Membrane Permeability
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Drosophila Proteins / chemistry
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Drosophila Proteins / genetics
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Drosophila Proteins / metabolism
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Gene Expression Regulation
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Genetic Predisposition to Disease
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Humans
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Ion Channel Gating
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Membrane Potentials
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Mice
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Mice, Knockout
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Phenotype
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Protein Conformation
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Protein Serine-Threonine Kinases / chemistry
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Protein Serine-Threonine Kinases / genetics
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Protein Serine-Threonine Kinases / metabolism
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Signal Transduction
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Structure-Activity Relationship
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TRPM Cation Channels / chemistry
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TRPM Cation Channels / deficiency
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TRPM Cation Channels / genetics
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TRPM Cation Channels / metabolism*
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Xenopus Proteins / chemistry
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Xenopus Proteins / genetics
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Xenopus Proteins / metabolism
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Zebrafish Proteins / chemistry
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Zebrafish Proteins / genetics
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Zebrafish Proteins / metabolism
Substances
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Drosophila Proteins
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TRPM Cation Channels
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TRPM protein, Drosophila
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TRPM7 protein, Xenopus
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Xenopus Proteins
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Zebrafish Proteins
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Trpm7 protein, mouse
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Protein Serine-Threonine Kinases
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TRPM7 protein, human
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Trpm7 protein, zebrafish