Direct binding between BubR1 and B56–PP2A phosphatase complexes regulate mitotic progression
Abstract
Summary: BubR1 is a central component of the spindle assembly checkpoint that inhibits progression into anaphase in response to improper kinetochore–microtubule interactions. In addition, BubR1 also helps stabilize kinetochore–microtubule interactions by counteracting the Aurora B kinase but the mechanism behind this is not clear. Here we show that BubR1 directly binds to the B56 family of protein phosphatase 2A (PP2A) regulatory subunits through a conserved motif that is phosphorylated by cyclin-dependent kinase 1 (Cdk1) and polo-like kinase 1 (Plk1). Two highly conserved hydrophobic residues surrounding the serine 670 Cdk1 phosphorylation site are required for B56 binding. Mutation of these residues prevents the establishment of a proper metaphase plate and delays cells in mitosis. Furthermore, we show that phosphorylation of serines 670 and 676 stimulates the binding of B56 to BubR1 and that BubR1 targets a pool of B56 to kinetochores. Our data suggest that BubR1 counteracts Aurora B kinase activity at improperly attached kinetochores by recruiting B56–PP2A phosphatase complexes.
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Previous studies showed that phosphorylation or negatively charged residues at positions 2, 7, 8 and 9 enhance B′ binding.
“Previous studies showed that phosphorylation or negatively charged residues at positions 2, 7, 8 and 9 enhance B′ binding [12, 17, 21].”
From PP2A-B′ holoenzyme substrate recognition, regulation and role in cytokinesis (2017) · cites this paper as [17]
Our study corroborates the previous results that phosphorylation or negatively charged residues at positions 2, 7, 8 and 9 enhance B′ binding.
“Our study also corroborates the previous results that phosphorylation or negatively charged residues at positions 2, 7, 8 and 9 enhance B′ binding [12, 17, 21].”
From PP2A-B′ holoenzyme substrate recognition, regulation and role in cytokinesis (2017) · cites this paper as [17]
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References 21 · Cited by 205
- Authors
- Kruse, T., Zhang, G., Larsen, M. S. Y., Lischetti, T., Streicher, W., Kragh Nielsen, T., Bjørn, S. P., & Nilsson, J.
- Affiliations
- University of Copenhagen (DK)
- The Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Blegdamsvej 3b, 2200 Copenhagen, Denmark
- Corresponding author
- Nilsson, Jakob
- ORCID
- Venue
- Journal of Cell Science
- Publisher
- The Company of Biologists
- Published
- 2013-03-01
- Volume
- 126
- Issue
- 5
- Pages
- 1086-1092
- ISSN
- 0021-9533 (ISSN-L)
- 1477-9137
- OpenAlex
- W2098759786
- Cited by
- 205
- References
- 21
- Citations by year
- 2026: 7 · 2025: 12 · 2024: 6 · 2023: 8 · 2022: 16 · 2021: 12 · 2020: 19 · 2019: 14 · 2018: 9 · 2017: 25 · 2016: 19 · 2015: 28 · 2014: 19 · 2013: 9 · 2012: 1
- FWCI
- 14.50
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Cell Science (publishedVersion)
- PubMed (publishedVersion)
- Research at the University of Copenhagen (University of Copenhagen) (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Biotin and Related Studies
- Keywords
- BubR1, protein phosphatase 2A, spindle assembly checkpoint, mitotic progression, CDK1 phosphorylation, PLK1 phosphorylation, Aurora B kinase, kinetochore-microtubule attachment, metaphase plate, protein-protein binding, mitosis
- MeSH terms
- Polo-Like Kinase 1, Chromatography, Gel, HeLa Cells, Humans, Microscopy, Fluorescence, Mitosis, Phosphorylation, Protein Binding, Proto-Oncogene Proteins, CDC2 Protein Kinase, Protein Serine-Threonine Kinases, Cell Cycle Proteins, Two-Hybrid System Techniques, Immunoprecipitation, Protein Phosphatase 2
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