Meister, A. & Anderson, M. E. Glutathione. Annu. Rev. Biochem. 52, 711–760 (1983).
Mårtensson, J., Lai, J. C. & Meister, A. High-affinity transport of glutathione is part of a multicomponent system essential for mitochondrial function. Proc. Natl Acad. Sci. USA 87, 7185–7189 (1990).
Deponte, M. The incomplete glutathione puzzle: just guessing at numbers and figures? Antioxid. Redox Signal. 27, 1130–1161 (2017).
Griffith, O. W. & Meister, A. Origin and turnover of mitochondrial glutathione. Proc. Natl Acad. Sci. USA 82, 4668–4672 (1985).
Hwang, C., Sinskey, A. J. & Lodish, H. F. Oxidized redox state of glutathione in the endoplasmic reticulum. Science 257, 1496–1502 (1992).
Meredith, M. J. & Reed, D. J. Status of the mitochondrial pool of glutathione in the isolated hepatocyte. J. Biol. Chem. 257, 3747–3753 (1982).
Deneke, S. M. & Fanburg, B. L. Regulation of cellular glutathione. Am. J. Physiol. Lung Cell. Mol. Physiol. 257, L163–L173 (1989).
Jones, D. P. Redox potential of GSH/GSSG couple: assay and biological significance. Methods Enzymol. 348, 93–112 (2002).
Kurosawa, K., Hayashi, N., Sato, N., Kamada, T. & Tagawa, K. Transport of glutathione across the mitochondrial membranes. Biochem. Biophys. Res. Commun. 167, 367–372 (1990).
Griffith, O. W. & Meister, A. Potent and specific inhibition of glutathione synthesis by buthionine sulfoximine (S-n-butyl homocysteine sulfoximine). J. Biol. Chem. 254, 7558–7560 (1979).
Münch, C. & Harper, J. W. Mitochondrial unfolded protein response controls matrix pre-RNA processing and translation. Nature 534, 710–713 (2016).
Lee, H.-R. et al. Adaptive response to GSH depletion and resistance to l-buthionine-(S,R)-sulfoximine: involvement of Nrf2 activation. Mol. Cell. Biochem. 318, 23–31 (2008).
Sun, X. et al. Activation of the p62–Keap1–NRF2 pathway protects against ferroptosis in hepatocellular carcinoma cells. Hepatology 63, 173–184 (2016).
Booty, L. M. et al. Selective disruption of mitochondrial thiol redox state in cells and in vivo. Cell Chem. Biol. 26, 449-461.e8 (2019).
Ruprecht, J. J. & Kunji, E. R. S. The SLC25 mitochondrial carrier family: structure and mechanism. Trends Biochem. Sci. 45, 244–258 (2020).
Pebay-Peyroula, E. et al. Structure of mitochondrial ADP/ATP carrier in complex with carboxyatractyloside. Nature 426, 39–44 (2003).
Zhu, X. G. et al. CHP1 regulates compartmentalized glycerolipid synthesis by activating GPAT4. Mol. Cell 74, 45–58.e7 (2019).
Zhang, H., Go, Y.-M. & Jones, D. P. Mitochondrial thioredoxin-2/peroxiredoxin-3 system functions in parallel with mitochondrial GSH system in protection against oxidative stress. Arch. Biochem. Biophys. 465, 119–126 (2007).
Seelig, G. F., Simondsen, R. P. & Meister, A. Reversible dissociation of gamma-glutamylcysteine synthetase into two subunits. J. Biol. Chem. 259, 9345–9347 (1984).
Li, W., Li, Z., Yang, J. & Ye, Q. Production of glutathione using a bifunctional enzyme encoded by gshF from Streptococcus thermophilus expressed in Escherichia coli. J. Biotechnol. 154, 261–268 (2011).
Chen, W. W., Freinkman, E., Wang, T., Birsoy, K. & Sabatini, D. M. Absolute quantification of matrix metabolites reveals the dynamics of mitochondrial metabolism. Cell 166, 1324–1337.e11 (2016).
Slabbaert, J. R. et al. Shawn, the Drosophila homolog of SLC25A39/40, is a mitochondrial carrier that promotes neuronal survival. J. Neurosci. 36, 1914–1929 (2016).
Usaj, M. et al. TheCellMap.org: a web-accessible database for visualizing and mining the global yeast genetic interaction network. Genes Genomes Genet. 7, 1539–1549 (2017).
Luk, E., Carroll, M., Baker, M. & Culotta, V. C. Manganese activation of superoxide dismutase 2 in Saccharomyces cerevisiae requires MTM1, a member of the mitochondrial carrier family. Proc. Natl Acad. Sci. USA 100, 10353–10357 (2003).
Nilsson, R. et al. Discovery of genes essential for heme biosynthesis through large-scale gene expression analysis. Cell Metab. 10, 119–130 (2009).
Biederbick, A. et al. Role of human mitochondrial Nfs1 in cytosolic iron–sulfur protein biogenesis and iron regulation. Mol. Cell. Biol. 26, 5675–5687 (2006).
Mayr, J. A., Feichtinger, R. G., Tort, F., Ribes, A. & Sperl, W. Lipoic acid biosynthesis defects. J. Inherit. Metab. Dis. 37, 553–563 (2014).
Chen, Z. & Lash, L. H. Evidence for mitochondrial uptake of glutathione by dicarboxylate and 2-oxoglutarate carriers. J. Pharmacol. Exp. Ther. 285, 608–618 (1998).
Booty, L. M. et al. The mitochondrial dicarboxylate and 2-oxoglutarate carriers do not transport glutathione. FEBS Lett. 589, 621–628 (2015).
Kumar, C. et al. Glutathione revisited: a vital function in iron metabolism and ancillary role in thiol-redox control. EMBO J. 30, 2044–2056 (2011).
Rodríguez-Manzaneque, M. T., Tamarit, J., Bellí, G., Ros, J. & Herrero, E. Grx5 is a mitochondrial glutaredoxin required for the activity of iron/sulfur enzymes. Mol. Biol. Cell 13, 1109–1121 (2002).
Almusafri, F. et al. Clinical and molecular characterization of 6 children with glutamate–cysteine ligase deficiency causing hemolytic anemia. Blood Cells. Mol. Dis. 65, 73–77 (2017).
Wessel, D. & Flügge, U. I. A method for the quantitative recovery of protein in dilute solution in the presence of detergents and lipids. Anal. Biochem. 138, 141–143 (1984).
McAlister, G. C. et al. MultiNotch MS3 enables accurate, sensitive, and multiplexed detection of differential expression across cancer cell line proteomes. Anal. Chem. 86, 7150–7158 (2014).
Tyanova, S. et al. The Perseus computational platform for comprehensive analysis of (prote)omics data. Nat. Methods 13, 731–740 (2016).
Birsoy, K. et al. An essential role of the mitochondrial electron transport chain in cell proliferation is to enable aspartate synthesis. Cell 162, 540–551 (2015).
Concordet, J.-P. & Haeussler, M. CRISPOR: intuitive guide selection for CRISPR/Cas9 genome editing experiments and screens. Nucleic Acids Res. 46, W242–W245 (2018).
Shola, D. T. N., Yang, C., Han, C., Norinsky, R. & Peraza, R. D. in Mouse Genetics: Methods and Protocols (eds. Singh, S. R., Hoffman, R. M. & Singh, A.) 1–27 (Springer US, 2021).
Murgha, Y. E., Rouillard, J.-M. & Gulari, E. Methods for the preparation of large quantities of complex single-stranded oligonucleotide libraries. PLoS ONE 9, e94752 (2014).
Sadreyev, I. R., Ji, F., Cohen, E., Ruvkun, G. & Tabach, Y. PhyloGene server for identification and visualization of co-evolving proteins using normalized phylogenetic profiles. Nucleic Acids Res. 43, W154–W159 (2015).
Ruan, J. et al. TreeFam: 2008 update. Nucleic Acids Res. 36, D735–D740 (2008).
Thomas, P. D. et al. PANTHER: a library of protein families and subfamilies indexed by function. Genome Res. 13, 2129–2141 (2003).
Studer, G. et al. ProMod3—a versatile homology modelling toolbox. PLOS Comput. Biol. 17, e1008667 (2021).
Pebay-Peyroula, E. et al. Structure of mitochondrial ADP/ATP carrier in complex with carboxyatractyloside. Nature 426, 39–44 (2003).
Robinson, A. J. & Kunji, E. R. S. Mitochondrial carriers in the cytoplasmic state have a common substrate binding site. Proc. Natl. Acad. Sci. 103, 2617–2622 (2006).
Pettersen, E. F. et al. UCSF Chimera—a visualization system for exploratory research and analysis. J. Comput. Chem. 25, 1605–1612 (2004).
Bycroft, C. et al. The UK Biobank resource with deep phenotyping and genomic data. Nature 562, 203–209 (2018).
Barbeira, A. N. et al. Integrating predicted transcriptome from multiple tissues improves association detection. PLoS Genet. 15, e1007889 (2019).
Zhou, D. et al. A unified framework for joint-tissue transcriptome-wide association and Mendelian randomization analysis. Nat. Genet. 52, 1239–1246 (2020).
Unlu, G. et al. Phenome-based approach identifies RIC1-linked Mendelian syndrome through zebrafish models, biobank associations and clinical studies. Nat. Med. 26, 98–109 (2020).
Aguet, F. et al. Genetic effects on gene expression across human tissues. Nature 550, 204–213 (2017).
More News
Daily briefing: Carrion crows have counting skills seen only in people
Researcher parents are paying a high price for conference travel — here’s how to fix it
Asymmetric hydrogenation of ketimines with minimally different alkyl groups – Nature