Abstract
Copper is an essential element in all forms of life. It acts as a cofactor of some enzymes and is involved in forming proper protein conformations. However, excess copper ions in cells are detrimental as they can generate free radicals or disrupt protein structures. Therefore, all life forms have evolved conserved and exquisite copper metabolic systems to maintain copper homeostasis. The yeast Saccharomyces cerevisiae has been widely used to investigate copper metabolism as it is convenient for this purpose. In this review, we summarize the mechanism of copper metabolism in Saccharomyces cerevisiae according to the latest literature. In brief, bioavailable copper ions are incorporated into yeast cells mainly via the high-affinity transporters Ctr1 and Ctr3. Then, intracellular Cu+ ions are delivered to different organelles or cuproproteins by different chaperones, including Ccs1, Atx1, and Cox17. Excess copper ions bind to glutathione (GSH), metallothioneins, and copper complexes are sequestered into vacuoles to avoid toxicity. Copper-sensing transcription factors Ace1 and Mac1 regulate the expression of genes involved in copper detoxification and uptake/mobilization in response to changes in intracellular copper levels. Though numerous recent breakthroughs in understanding yeast’s copper metabolism have been achieved, some issues remain unresolved. Completely elucidating the mechanism of copper metabolism in yeast helps decode the corresponding system in humans and understand how copper-related diseases develop.
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This work was supported by the National Natural Science Foundation of China (91749121 to Li), the Fundamental Research Funds for Central Universities (SCU2019D013 to Li and SCU2019C4005 to Shi), and the Outstanding Young and Middle-aged Scientific and Technological Innovation Team Program of the Colleges and Universities in Hubei Province (T201819 to Jiang).
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Shi, H., Jiang, Y., Yang, Y. et al. Copper metabolism in Saccharomyces cerevisiae: an update. Biometals 34, 3–14 (2021). https://doi.org/10.1007/s10534-020-00264-y
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DOI: https://doi.org/10.1007/s10534-020-00264-y