Magnesium transporters are proteins that transport magnesium across the cell membrane. All forms of life require magnesium, yet the molecular mechanisms of Mg2+ uptake from the environment and the distribution of this vital element within the organism are only slowly being elucidated. The ATPase function of MgtA is highly cardiolipin dependent and has been shown to detect free magnesium in the μM range In bacteria, Mg2+ is probably mainly supplied by the CorA protein and, where the CorA protein is absent, by the MgtE protein. In yeast the initial uptake is via the Alr1p and Alr2p proteins, but at this stage the only internal Mg2+ distributing protein identified is Mrs2p. Within the protozoa only one Mg2+ transporter (XntAp) has been identified. In metazoa, Mrs2p and MgtE homologues have been identified, along with two novel Mg2+ transport systems TRPM6/TRPM7 and PCLN-1. Finally, in plants, a family of Mrs2p homologues has been identified along with another novel protein, AtMHX. Evolution The evolution of Mg2+ transport appears to have been rather complicated. Proteins apparently based on MgtE are present in bacteria and metazoa, but are missing in fungi and plants, whilst proteins apparently related to CorA are present in all of these groups. The two active transport transporters present in bacteria, MgtA and MgtB, do not appear to have any homologies in higher organisms. There are also Mg2+ transport systems that are found only in the higher organisms. Types There are a large number of proteins yet to be identified that transport Mg2+. Even in the best studied eukaryote, yeast, Borrelly has reported a Mg2+/H+ exchanger without an associated protein, which is probably localised to the Golgi. At least one other major Mg2+ transporter in yeast is still unaccounted for, the one affecting Mg2+ transport in and out of the yeast vacuole. In higher, multicellular organisms, it seems that many Mg2+ transporting proteins await discovery. The CorA-domain-containing Mg2+ transporters (CorA, Alr-like and Mrs2-like) have a similar but not identical array of affinities for divalent cations. In fact, this observation can be extended to all of the Mg2+ transporters identified so far. This similarity suggests that the basic properties of Mg2+ strongly influence the possible mechanisms of recognition and transport. However, this observation also suggests that using other metal ions as tracers for Mg2+ uptake will not necessarily produce results comparable to the transporter's ability to transport Mg2+. Ideally, Mg2+ should be measured directly.