ArticleJournal of cell science2012
MLL5 maintains genomic integrity by regulating the stability of the chromosomal passenger complex through a functional interaction with Borealin.
Article in Journal of cell science, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
8 citing papers in PubMed.
- Defining Biological and Biochemical Functions of Noncanonical SET Domain Proteins.Journal of molecular biology · 2024Review
- Case Report:Frontiers in pediatrics · 2021Article
- SET domains and stress: uncovering new functions for yeast Set4.Current genetics · 2019Review
- MLL5 (KMT2E): structure, function, and clinical relevance.Cellular and molecular life sciences : CMLS · 2017Review
- MLL5 maintains spindle bipolarity by preventing aberrant cytosolic aggregation of PLK1.The Journal of cell biology · 2016Article
- Mouse BRWD1 is critical for spermatid postmeiotic transcription and female meiotic chromosome stability.The Journal of cell biology · 2015Article
- Molecular basis for chromatin binding and regulation of MLL5.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Article
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Authors and funding
3 authors.
Funding
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Abstract
Mixed lineage leukemia 5 (MLL5) is a versatile nuclear protein associated with many cellular events. We have shown previously that phosphorylation of MLL5 by Cdk1 is required for mitotic entry. In this paper, the function of MLL5 in mitotic regulation is further explored. SiRNA-mediated downregulation of MLL5 caused improper chromosome alignment at metaphase and resulted in failure of DNA segregation and cytokinesis. Mechanistic studies revealed that the chromosomal passenger complex (CPC), which plays a key role in chromosomal bi-orientation, was delocalized from the inner centromere region because of proteasome-mediated degradation in MLL5-depleted cells. Biochemical analyses further demonstrated that the central domain of MLL5 interacted with the C-terminus of Borealin, and the interaction is essential to maintain the stability of Borealin. Moreover, the mitotic defects in MLL5-depleted cells were rescued by overexpression of FLAG-MLL5, but not by a FLAG-MLL5 mutant that did not contain the central domain. Collectively, our results suggest that MLL5 functionally interacts with Borealin, facilitates the expression of CPC, and hence contributes to mitotic fidelity and genomic integrity.
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