| First Author | Ryazanova LV | Year | 2010 |
| Journal | Nat Commun | Volume | 1 |
| Pages | 109 | PubMed ID | 21045827 |
| Mgi Jnum | J:205665 | Mgi Id | MGI:5545986 |
| Doi | 10.1038/ncomms1108 | Citation | Ryazanova LV, et al. (2010) TRPM7 is essential for Mg(2+) homeostasis in mammals. Nat Commun 1:109 |
| abstractText | Mg(2+) is the second-most abundant cation in animal cells and is an essential cofactor in numerous enzymatic reactions. The molecular mechanisms controlling Mg(2+) 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 Mg(2+) homeostasis in mammals. We generated TRPM7-deficient mice with the deletion of the kinase domain. Homozygous TRPM7(Deltakinase) mice demonstrated early embryonic lethality, whereas heterozygous mice were viable, but developed signs of hypomagnesaemia and revealed a defect in intestinal Mg(2+) absorption. Cells derived from heterozygous TRPM7(Deltakinase) mice demonstrated reduced TRPM7 currents that had increased sensitivity to the inhibition by Mg(2+). Embryonic stem cells lacking TRPM7 kinase domain displayed a proliferation arrest phenotype that can be rescued by Mg(2+) supplementation. Our results demonstrate that TRPM7 is essential for the control of cellular and whole body Mg(2+) homeostasis. |
