Magnesium and Mg2+ Transport Proteins in Cells

This is the authors' abstract. We don't add key points for this paper.

Magnesium is one of the most important and abundant divalent cations in living cells. Organisms must maintain physiological levels of Mg2+ because this divalent cation is critical for the stabilization of membranes and ribosomes and for the neutralization of nucleic acids. Over 300 enzymes are known to be Mg-dependent. The cellular concentration of Mg2+ is regulated by transmembrane pathways. Prokaryotes carry three classes of Mg2+ transport systems: CorA, MgtE, and MgtA. Some of eukaryotic Mg2+ transport proteins have some similarity to those found in prokaryotes. Mitochondrial RNA splicing protein 2 (MRS2) shares many of properties of the bacterial CorA protein. The Solute Carrier Family 41 Member 1 (SLC41A1) and Cyclin and CBS Domain Divalent Metal Cation Transport Mediator (CNNM) family proteins have a similarity with some regions of the bacterial MgtE and CorC proteins, respectively. Mammalian Mg2+ homeostasis is also regulated by Mg2+ transport proteins including Transient Receptor Potential Cation Channel Subfamily M, Member 6/7 (TRPM6/7), Claudin-16, Magnesium Transporter 1 (MAGT1), and Nonimprinted in Prader-Willi/Angelman Syndrome Region (NIPA) proteins that are not represented in prokaryotic genomes. These eukaryotic Mg2+ transport proteins have no obvious amino acid sequence similarities, indicating that there are many ways to transport Mg2+ across membranes.