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. 2020 Sep 23;11(9):789. doi: 10.1038/s41419-020-02994-w

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© The Author(s) 2020

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 3 — Cysteine and cystine can be transported via Na⁺-dependent and Na⁺-independent transporters. Cystine imported by xCT and/or BAT1 is reduced in the intracellular milieu by GSH or thioredoxin. Alternatively, reduced form of cysteine can be directly imported or produced from homocysteine via the transsulfuration pathway. Cysteine is incorporated into GSH via the actions of γ-glutamylcysteine ligase (GCL) and glutathione synthetase (GS). Once oxidised, GSH is exported outside the cell via multidrug-resistance protein (MRP), where it is cleaved by the actions of GGT and a dipeptidase (DP). The cell can take each of the products of GSH cleavage, individually or as a dipeptide (γ-glutamyl cycle). Alternatively, GSH can be cleaved inside the cell by the action of CHAC and DP, that way serving as a cysteine intracellular pool. This figure was created using Servier Medical Art templates, which are licensed under a Creative Commons Attribution 3.0 Unported License; https://smart.servier.com.