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. 2020 Aug 13;11:4046. doi: 10.1038/s41467-020-17862-6

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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. 6 — Working model for functional lipoylation of the OGDHc. a Cyclical reduction and oxidation of lipoate is required for OGDHc catalytic activity, and this process requires ABHD11 which associates with the OGDHc, maintaining functional lipoylation and allowing the conversion of 2-OG to succinyl CoA. b When ABHD11 is depleted or inhibited, lipoyl adducts form, preventing functional lipoylation. These adducts may arise from lipid peroxidation products (e.g. 4-HNE) formed by ROS generated by the OGDHc or by the electron transport chain, or by other as yet undefined mechanisms. Loss of functional lipoylation leads to 2-OG accumulation and the formation of L-2-HG, which can inhibit 2-OG dependent dioxygenases involved in the HIF response and DNA hydroxymethylation.