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. 2025 Jul 15;26(17):4219–4247. doi: 10.1038/s44319-025-00523-4

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© The Author(s) 2025

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 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/. Creative Commons Public Domain Dedication waiver http://creativecommons.org/publicdomain/zero/1.0/ applies to the data associated with this article, unless otherwise stated in a credit line to the data, but does not extend to the graphical or creative elements of illustrations, charts, or figures. This waiver removes legal barriers to the re-use and mining of research data. According to standard scholarly practice, it is recommended to provide appropriate citation and attribution whenever technically possible.

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(A) A Coulombic electrostatic potential map of the CPC targeting module in complex with an H3pT3 nucleosome. PDB ID 8RUQ, EMDB ID—EMD-19514, Table EV1A (all particles). (B) The borealin N-terminus (white) interacts with the acidic patch (black outline indicates idealised surface) formed by H2A (red) and H2B (yellow). Numbers indicate three areas of interest. (C) Details of the interactions between the borealin N-terminus (grey/white) and different regions 1–3 of the nucleosome acidic patch. (D) EMSAs between 150 nM H3pT3 phosphorylated nucleosomes and CPC80-Bor_(1-76) targeting module complexes containing borealin_1-76 wild-type, R9A, K12A or R9A-K12A mutations at the specified molar excess. (E) Dependence of MPS1 kinetochore localisation (MPS1^KT), pericentromeric enrichment of borealin-mScarlet (borealin^pcen) and H3pS10 on chromatin were tested in HeLa Flp-In T-REx MPS1-GFP cells using siRNA depletion and rescue assays for wild-type borealin, an N-terminal deletion lacking the first nine amino acids (10–280) and an N-terminal deletion lacking the first nine amino acids and the C-terminal dimerization domain (10–221). Representative images with 10 µm scale bars are shown. (F) scatter plots with mean ± SEM for MPS1^KT, borealin^pcen and H3pS10 and a Kruskal–Wallis test and Dunn’s test for multiple comparisons for significance for comparisons indicated in the graphs. For MPS1^KT, No rescue vs WT P < 0.0001 (****), WT vs 10–281 P = 0.4744 (ns) and WT vs 10–221 P = 0.0053 (**). For Borealin^pcen, No rescue vs WT P < 0.0001 (****), WT vs 10–281 P = 0.0244 (*) and WT vs 10–221 P = 0.0001 (***). For H3pS10, No rescue vs WT P < 0.0001 (****), WT vs 10–281 P = 0.0006 (***) and WT vs 10–221 P < 0.0001 (***). Sample sizes (F) n > 20 cells MPS1, n > 20 cells borealin, n > 23 cells H3pS10 from at least three independent experiments.