Chubanov, Vladimir and Waldegger, Siegfried and Schnitzler, Michael Mederos y and Vitzthum, Helga and Sassen, Martin C. and Seyberth, Hannsjörg W. and Konrad, Martin and Gudermann, Thomas (2004) Disruption of TRPM6/TRPM7 complex formation by a mutation in the TRPM6 gene causes hypomagnesemia with secondary hypocalcemia. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 101 (9). pp. 2894-2899. ISSN 0027-8424
Full text not available from this repository. (Request a copy)Abstract
Impaired magnesium reabsorption in patients with TRPM6 gene mutations stresses an important role of TRPM6 (melastatin-related TRP cation channel) in epithelial magnesium transport. While attempting to isolate full-length TRPM6, we found that the human TRPM6 gene encodes multiple mRNA isoforms. Full-length TRPM6 variants failed to form functional channel complexes because they were retained intracellularly on heterologous expression in HEK 293 cells and Xenopus oocytes. However, TRPM6 specifically interacted with its closest homolog, the Mg2+-permeable cation channel TRPM7, resulting in the assembly of functional TRPM6/TRPM7 complexes at the cell surface. The naturally occurring S141L TRPM6 missense mutation abrogated the oligomeric assembly of TRPM6, thus providing a cell biological explanation for the human disease. Together, our data suggest an important contribution of TRPM6/TRPM7 heterooligomerization for the biological role of TRPM6 in epithelial magnesium absorption.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | RECEPTOR POTENTIAL CHANNELS; MAGNESIUM TRANSPORT; CATION CHANNEL; PROTEIN; BRAIN; |
| Subjects: | 500 Science > 570 Life sciences 600 Technology > 610 Medical sciences Medicine |
| Divisions: | Biology, Preclinical Medicine > Institut für Physiologie |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 21 Jul 2021 10:51 |
| Last Modified: | 21 Jul 2021 10:51 |
| URI: | https://pred.uni-regensburg.de/id/eprint/37889 |
Actions (login required)
 |
View Item |
