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- W1970646502 abstract "Transient receptor potential (TRP) family channels are involved in sensory pathways and are activated by various environmental stimuli. Among the members of this family, TRPM7 is a unique fusion of an ion channel and a C-terminus kinase domain that is ubiquitously expressed. TRPM7 is a key membrane protein governing cellular Mg2+ homeostasis in mammals since its channel pore is permeable to Mg2+ ions and can act as a Mg2+ influx pathway. Moreover, TRPM7 channel activity is inhibited by intracellular Mg2+. Mechanistic links between its kinase activity and channel function have remained uncertain, partly due to embryonic lethality of TRPM7 gene deletion in mice. In this study, we generated kinase inactive knock-in mutant mice by mutagenesis of a key lysine residue involved in Mg2+-ATP binding. K1646R mutant mice were normal in development and general locomotor activity. In peritoneal macrophages isolated from adult animals the basal activity of TRPM7 channels prior to cytoplasmic Mg2+ depletion was significantly potentiated, while maximal current densities measured after Mg2+ depletion were unchanged in the absence of detectable kinase function. The inhibition of TRPM7 channel currents by 300 uM intracellular Mg2+ or spermine was similar in WT and K1646R macrophages. Serum total Ca2+ and Mg2+ levels were not significantly altered in kinase-dead mutant mice either. Our findings suggest that 1) abolishing TRPM7 kinase activity does not impair its channel activity, but rather, potentiates basal current magnitudes; 2) kinase activity is not essential for regulation of mammalian Mg2+ homeostasis." @default.
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- W1970646502 date "2015-01-01" @default.
- W1970646502 modified "2023-09-29" @default.
- W1970646502 title "Effects of Inactivation of TRPM7 Kinase Activity on its Channel Activity in Mice" @default.
- W1970646502 doi "https://doi.org/10.1016/j.bpj.2014.11.232" @default.
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