Abstract
A host of critical metalloproteins reside in mitochondria, where metallation occurs within the organelle after protein import. Although the pathways by which proteins are imported into the mitochondria are well known, the mechanisms by which their metal partners are imported are more obscure. A new study by Boulet et al. demonstrates that the mammalian SLC25A3 inner membrane transporter, previously known as a phosphate carrier, is also a functional Cu(I) importer, clarifying the source of mitochondrial copper and raising new questions about cellular copper homeostasis.
Highlights
Metalloenzymes and metalloproteins containing iron, zinc, copper, or manganese ions as cofactors are required in mitochondria to maintain normal physiology
Copper is required within the mitochondrion for the function of two metalloenzymes, c oxidase (COX) and superoxide dismutase-1 (SOD1)
Copper metallation of these two enzymes occurs within the mitochondrial intermembrane space (IMS) and is mediated by metallochaperone proteins, the source of the copper is a labile copper-ligand pool localized to the matrix (5)
Summary
Metalloenzymes and metalloproteins containing iron, zinc, copper, or manganese ions as cofactors are required in mitochondria to maintain normal physiology. Copper metallation of these two enzymes occurs within the mitochondrial intermembrane space (IMS) and is mediated by metallochaperone proteins, the source of the copper is a labile copper-ligand pool localized to the matrix (5). Studies in yeast demonstrated that Pic[2], another mitochondrial carrier protein, contributed to copper uptake (6).
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