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. 2020 Aug 3;20:291. doi: 10.1186/s12883-020-01873-3

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© The Author(s) 2020

Open AccessThis 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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

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Fig. 3 — Model for the role of ARH3 (encoded by the ADPRHL2 gene) in PAR degradation and apoptosis-inducing factor-mediated cell death. The PARP1 activation triggered by DNA damage leads to poly-ADP ribosylation of PARP1 and other acceptor proteins in the nucleus. Poly (ADP-ribose) glycohydrolase (PARG) hydrolyzes PAR added to the target protein, e.g. PARP1, hence facilitating the protein’s translocation to the cytoplasm and mitochondria. ARH3 hydrolyzes PAR. In the nucleus, AIF recruits various nucleases, e.g. cyclophilin A and H2AX, leading to large-scale DNA fragmentation. There is a general belief that ARH3 is also located in the mitochondrial matrix. The figure is redrawn from [32]