TRPM6 and TRPM7 differentially contribute to the relief of heteromeric TRPM6/7 channels from inhibition by cytosolic Mg²⁺ and Mg·ATP.

ABSTRACT: TRPM6 and its homologue TRPM7 are α-kinase-coupled divalent cation-selective channels activated upon reduction of cytosolic levels of Mg²⁺ and Mg·ATP. TRPM6 is vital for organismal Mg²⁺ balance. However, mechanistically the cellular role and functional nonredundancy of TRPM6 remain incompletely understood. Comparative analysis of native currents in primary cells from TRPM6- versus TRPM7-deficient mice supported the concept that native TRPM6 primarily functions as a constituent of heteromeric TRPM6/7 channels. However, heterologous expression of the human TRPM6 protein engendered controversial results with respect to channel characteristics including its regulation by Mg²⁺ and Mg·ATP. To resolve this issue, we cloned the mouse TRPM6 (mTRPM6) cDNA and compare

SUBMITTER: Ferioli S 

PROVIDER: S-EPMC5562840 | biostudies-literature | 2017 Aug

REPOSITORIES: biostudies-literature