Filling the mitochondrial copper pool

The Journal of Biological Chemistry
Dennis R Winge

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.

References

Jan 20, 2004·The Journal of Biological Chemistry·Paul A CobineDennis R Winge
Sep 30, 2006·The Journal of Biological Chemistry·Paul A CobineDennis R Winge
Feb 12, 2011·Blood·Marie-Berengere TroadecJerry Kaplan
Jul 23, 2011·The Biochemical Journal·Heeyong YoonAndrew Dancis
May 7, 2014·Journal of Inherited Metabolic Disease·Ferdinando Palmieri
Jan 15, 2016·Open Biology·Katherine E VestPaul A Cobine

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Citations

Jan 1, 2020·Antioxidants & Redox Signaling·Xin HuDean P Jones
Oct 23, 2020·Biochimica Et Biophysica Acta. Molecular Cell Research·Vinit C ShanbhagMichael J Petris

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