TRPM7 is essential for Mg2+ homeostasis in mammals

Lillia V. Ryazanova, Lusliany J. Rondon, Susanna Zierler, Zhixian Hu, Joanna Galli, Terry P. Yamaguchi, Andrzej Mazur, Andrea Fleig and Alexey G. Ryazanov ()
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Lillia V. Ryazanova: University of Medicine and Dentistry of New Jersey/R. W. Johnson Medical School
Lusliany J. Rondon: INRA, UMR 1019, UNH, CRNH Auvergne, and Clermont Université, Université d'Auvergne, Unité de Nutrition Humaine, BP 10448, Clermont-Ferrand F-63000, France.
Susanna Zierler: Laboratory of Cell and Molecular Signaling, Queen's Center for Biomedical Research, The Queen's Medical Center and John A. Burns School of Medicine, University of Hawaii
Zhixian Hu: University of Medicine and Dentistry of New Jersey/R. W. Johnson Medical School
Joanna Galli: INRA, UMR 1019, UNH, CRNH Auvergne, and Clermont Université, Université d'Auvergne, Unité de Nutrition Humaine, BP 10448, Clermont-Ferrand F-63000, France.
Terry P. Yamaguchi: Cancer and Developmental Biology Laboratory, Center for Cancer Research, National Cancer Institute-Frederick, NIH
Andrzej Mazur: INRA, UMR 1019, UNH, CRNH Auvergne, and Clermont Université, Université d'Auvergne, Unité de Nutrition Humaine, BP 10448, Clermont-Ferrand F-63000, France.
Andrea Fleig: Laboratory of Cell and Molecular Signaling, Queen's Center for Biomedical Research, The Queen's Medical Center and John A. Burns School of Medicine, University of Hawaii
Alexey G. Ryazanov: University of Medicine and Dentistry of New Jersey/R. W. Johnson Medical School

Nature Communications, 2010, vol. 1, issue 1, 1-9

Abstract: Abstract Mg2+ is the second-most abundant cation in animal cells and is an essential cofactor in numerous enzymatic reactions. The molecular mechanisms controlling Mg2+ balance in the organism are not well understood. In this study, we report identification of TRPM7, a bifunctional protein containing a protein kinase fused to an ion channel, as a key regulator of whole body Mg2+ homeostasis in mammals. We generated TRPM7-deficient mice with the deletion of the kinase domain. Homozygous TRPM7Δkinase mice demonstrated early embryonic lethality, whereas heterozygous mice were viable, but developed signs of hypomagnesaemia and revealed a defect in intestinal Mg2+ absorption. Cells derived from heterozygous TRPM7Δkinase mice demonstrated reduced TRPM7 currents that had increased sensitivity to the inhibition by Mg2+. Embryonic stem cells lacking TRPM7 kinase domain displayed a proliferation arrest phenotype that can be rescued by Mg2+ supplementation. Our results demonstrate that TRPM7 is essential for the control of cellular and whole body Mg2+ homeostasis.

Date: 2010
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DOI: 10.1038/ncomms1108

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