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. 2023 Feb 2;19(4):507–517. doi: 10.1038/s41589-022-01244-8

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© The Author(s) 2023

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. 6 — a, Overall persulfidation levels in HEK293 MSR cells before and after depletion of MPST (left panel). Cells were treated with 5 mM l-Cys for 30 min or were left untreated (UT). Relative persulfidation levels are indicated by Coomassie-normalized fluorescence intensity (right panel). Data are presented as mean and individual values (n = 3 biologically independent experiments) ± s.e.m. Statistical analysis based on a two-tailed unpaired t-test. b, Overall persulfidation levels in HEK293 MSR cells ectopically overexpressing roGFP2, MPST-roGFP2 or MPST(C248S)-roGFP2 (MPSTmut-roGFP2) (left panel). Relative persulfidation levels are indicated by Coomassie-normalized fluorescence intensity (right panel). Data are presented as mean and individual values (n = 3 biologically independent experiments) ± s.e.m. Statistical analysis based on a two-tailed unpaired t-test. c, Influence of MPST depletion on the persulfidation of individual proteins. Proteins depleted by at least twofold in MPST-depleted cells are marked in red. d, Interaction analysis of candidate MPST target proteins. Edges represent experimentally supported protein–protein interactions (confidence score >0.4) acquired from the STRING database⁵⁰. The graph was generated with Cytoscape⁵¹. e–g, Summary of MPST-driven transpersulfidation. The MPST-bound persulfide (MPST-SSH) sulfurates thiol-containing molecules, the outcome depending on the type of acceptor. e, Sulfur transfer to proteins (P) with vicinal dithiols (roGFP2, Trx1) generates a protein disulfide and releases H₂S. f, Sulfur transfer to protein monothiols leads to longer-lived protein persulfides. g, Sulfur transfer to GSH generates GSSH, which releases H₂S to generate GSSG or (dotted lines) to glutathionylate proteins.

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