ArticleCell cycle (Georgetown, Tex.)2019
Aurora kinase B-phosphorylated HP1α functions in chromosomal instability.
Article in Cell cycle (Georgetown, Tex.), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 14 citations in OpenAlex.
- Review
- Emergent properties of the lysine methylome reveal regulatory roles via protein interactions and histone mimicry.Epigenomics · 2025Article
- Writers and readers of H3K9me2 form distinct protein networks during the cell cycle that include candidates for H3K9 mimicry.Bioscience reports · 2023Article
- Cell division cycle-associated 8 is a prognostic biomarker related to immune invasion in hepatocellular carcinoma.Cancer medicine · 2023Article
- Borealin directs recruitment of the CPC to oocyte chromosomes and movement to the microtubules.The Journal of cell biology · 2021Article
- How HP1 Post-Translational Modifications Regulate Heterochromatin Formation and Maintenance.Cells · 2020Review
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Authors and funding
10 authors at 4 institutions in 4 countries.
Funding
Abstract
Heterochromatin Protein 1 α (HP1α) associates with members of the chromosome passenger complex (CPC) during mitosis, at centromeres where it is required for full Aurora Kinase B (AURKB) activity. Conversely, recent reports have identified AURKB as the major kinase responsible for phosphorylation of HP1α at Serine 92 (S92) during mitosis. Thus, the current study was designed to better understand the functional role of this posttranslationally modified form of HP1α. We find that S92-phosphorylated HP1α is generated in cells at early prophase, localizes to centromeres, and associates with regulators of chromosome stability, such as Inner Centromere Protein, INCENP. In mouse embryonic fibroblasts, HP1α knockout alone or reconstituted with a non-phosphorylatable (S92A) HP1α mutant results in mitotic chromosomal instability characterized by the formation of anaphase/telophase chromatin bridges and micronuclei. These effects are rescued by exogenous expression of wild type HP1α or a phosphomimetic (S92D) variant. Thus, the results from the current study extend our knowledge of the role of HP1α in chromosomal stability during mitosis.
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