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. 2018 Sep 26;9:3932. doi: 10.1038/s41467-018-06186-1

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© The Author(s) 2018

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. 7 — Model for PR-DUB regulation and its disruption in human cancers. a The 1:1 PR-DUB complex is first targeted to nucleosomal arrays either via the PHD domain of ASX-like proteins or through interactions with transcription factors and/or other binding partners (left). Enrichment of multiple 1:1 complexes in specific genomic regions increases the local PR-DUB concentration, favouring Calypso/BAP1 dimerisation and formation of a bidentate PR-DUB complex (middle). With bidentate complex formation, two C-terminal positively charged tails of Calypso/BAP1 are optimally oriented, enhancing nucleosome recruitment and efficient removal of H2AK119Ub (right). b Distinct classes of human PR-DUB mutations can impair PR-DUB targeting, recruitment, and activity on nucleosomes via multiple mechanisms