Regular ArticleThe Human Mitochondrial Mrs2 Protein Functionally Substitutes for Its Yeast Homologue, A Candidate Magnesium Transporter☆
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Cited by (98)
Recent Advances in the Structural Biology of Mg<sup>2+</sup> Channels and Transporters
2022, Journal of Molecular BiologyCitation Excerpt :Similar to the SLC41 family, the CNNM family transporters have also been reported to localize at the basolateral membrane with Na+-driven Mg2+ efflux activity.13,17 Finally, Mrs2 is a mitochondrial inner membrane protein that mediates essential Mg2+ transport for mitochondrial metabolic functions.18–19 Structural information is required to understand the Mg2+ transport mechanisms associated with these channel and transporter proteins (Figure 1(B)-1(E)), but only a few structures of prokaryotic origin, such as the crystal structures of CorA (bacterial homologue of Mrs2)20–24 and MgtE (bacterial homologue of SLC41),25–26 were available until recently.
Mineral requirements for mitochondrial function: A connection to redox balance and cellular differentiation
2022, Free Radical Biology and MedicineMitochondrial osmoregulation in evolution, cation transport and metabolism
2021, Biochimica et Biophysica Acta - BioenergeticsCitation Excerpt :As with other cations, mitochondrial Mg2+ levels are governed against the electrochemical equilibrium by inward and outward fluxes. The inward fluxes are mediated in dependence of the membrane potential by MRS2, the first molecularly identified mitochondrial cation transporter [121,122]. Mg2+ efflux has been proposed to work in exchange for ATP, H+ or Na+, and the Mg2+/Na+ carrier SLC41A3 is the only mitochondrial Mg2+ efflux system identified to date [123] (Fig. 1A).
A novel mitochondrial carrier protein Mme1 acts as a yeast mitochondrial magnesium exporter
2015, Biochimica et Biophysica Acta - Molecular Cell ResearchCitation Excerpt :The decrease in mitochondrial Mg2 + content of the mrs2Δ mutant can be rescued by the expression of bacterial Mg2 + transporter CorA fused to a mitochondrial N-terminal leader sequence of MRS2 [13]. The functional complementation was also observed with the orthologue of Mrs2 in humans [14]. Yeast Lpe10 also localizes at the mitochondrial inner membrane and shares 32% of its sequence identity and a conserved GMN motif with Mrs2 [15].
The structure and regulation of magnesium selective ion channels
2013, Biochimica et Biophysica Acta - BiomembranesMembrane protein interactions between different Arabidopsis thaliana MRS2-type magnesium transporters are highly permissive
2013, Biochimica et Biophysica Acta - BiomembranesCitation Excerpt :The gene and protein designations in yeast and bacteria reflect the initially observed phenotypes (e.g. CorA: cobalt resistance, MRS2: mitochondrial RNA splicing, ALR: aluminium resistance or MNR: manganese resistance) when the respective genes encoding 2-TM-GMN proteins are defect or over-expressed [3–7]. Their key function, however, is obviously the transport of Mg2 + across biological membranes, as conclusively demonstrated by their ability to complement defects of magnesium transport in respective mutants of the diverse genetic systems even across wide phylogenetic distances [8–14]. Moreover, a high-conductance (~ 155 pS) Mg2 + flux was demonstrated directly in single-channel patch clamping experiments of MRS2 in giant lipid vesicles [15,16].
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Sequence data from this article have been deposited with the EMBL/GenBank Data Libraries under Accession Nos. AF293076–AF293078.
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