TRPM7.

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.

• Authors: Andrea Fleig, Vladimir Chubanov
• Journal: Handbook of experimental pharmacology (Handb Exp Pharmacol) Vol. 222 Pg. 521-46 ( 2014) ISSN: 0171-2004 [Print] Germany
• PMID: 24756720 (Publication Type: Journal Article, Research Support, N.I.H., Extramural, Review)

Chemical References

• Drosophila Proteins
• TRPM Cation Channels
• TRPM protein, Drosophila
• TRPM7 protein, Xenopus
• Xenopus Proteins
• Zebrafish Proteins
• Trpm7 protein, mouse
• Protein Serine-Threonine Kinases
• TRPM7 protein, human
• Trpm7 protein, zebrafish

Topics

• Animals
• Cell Membrane Permeability
• Drosophila Proteins (chemistry, genetics, metabolism)
• Gene Expression Regulation
• Genetic Predisposition to Disease
• Humans
• Ion Channel Gating
• Membrane Potentials
• Mice
• Mice, Knockout
• Phenotype
• Protein Conformation
• Protein Serine-Threonine Kinases (chemistry, genetics, metabolism)
• Signal Transduction
• Structure-Activity Relationship
• TRPM Cation Channels (chemistry, deficiency, genetics, metabolism)
• Xenopus Proteins (chemistry, genetics, metabolism)
• Zebrafish Proteins (chemistry, genetics, metabolism)