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A highly conserved binding pocket on PP2A-B56 is required for shugoshin binding and cohesion protection
Open accessPreprint — published as 10.15252/embr.202052295 · Paper page
Abstract
The shugoshin proteins are universal protectors of centromeric cohesin during mitosis and meiosis. The binding of human Sgo1 to the PP2A-B56 phosphatase through a coiled coil (CC) region is believed to mediate cohesion protection during mitosis. Here we undertook a structure function analysis of the PP2A-B56-Sgo1 complex, revealing unanticipated aspects of complex formation and function. We establish that a highly conserved pocket of the B56 regulatory subunit is required for Sgo1 binding and cohesion protection. Consistent with this, we show that Sgo1 blocks the binding of PP2A-B56 substrates containing a canonical B56 binding motif. Surprisingly, we identify B56 and Sgo1 mutants that prevent complex formation yet support cohesion protection and normal mitotic progression. This suggests that Sgo1 and PP2A-B56 have cohesion protection activity independently of complex formation. Collectively our work provides important insight into cohesion protection during mitosis.
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Cites
Global quantification of mammalian gene expression control
Schwanhäusser, B., Busse, D., Li, N., Dittmar, G., Schuchhardt, J., Wolf, J., Chen, W., & Selbach, M. (2011) · Nature · doi:10.1038/nature10098 · Cited by 6,566
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Metadata
- Authors
- Ueki, Y., Hadders, M., Weisser, M. B., Nasa, I., Gupta, T., Hertz, E. T., Kruse, T., Montoya, G., Jeyaprakash, A. A., Kettenbach, A., Lens, S. M. A., & Nilsson, J.
- Affiliations
- University of Copenhagen (DK)
- Utrecht University (NL)
- Dartmouth College (US)
- Wellcome Centre for Cell Biology (GB)
- Corresponding author
- Nilsson, Jakob
- ORCID
- Venue
- EMBO Reports
- Publisher
- openRxiv
- Published
- 2020-12-19
- Volume
- 22
- Issue
- 7
- Pages
- e52295-e52295
- ISSN
- 1469-221X (ISSN-L)
- PMC
- PMC8256288
- OpenAlex
- W3161253920
- Cited by
- 16
- References
- 1
- Citations by year
- 2026: 4 · 2025: 2 · 2024: 1 · 2023: 5 · 2022: 3 · 2021: 1
- FWCI
- 1.31
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- EMBO Reports (publishedVersion, other-oa)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Research at the University of Copenhagen (University of Copenhagen) (publishedVersion, cc-by)
- Edinburgh Research Explorer (University of Edinburgh) (submittedVersion, cc-by)
- Utrecht University Repository (Utrecht University) (submittedVersion, other-oa)
- Funders
- Kræftens Bekæmpelse (R167-A10951-17-S2)
- Wellcome Trust (202811/Z/16/Z, 202811, 202811202811, 095822)
- Danish Cancer Society Research Center (R167- A10951-17-S2)
- Lundbeckfonden (NNF14CC0001, 2017-3212, R167-)
- Novo Nordisk (NNF14CC0001, NNF17SA0030214, NNF0024386)
- KWF Kankerbestrijding (10366)
- Novo Nordisk Fonden (NNF 14CC0001, NNF0024386, NNF17SA0030214, (grant NNF14CC0001), NNF18OC0053124)
- Oncode Institute
- Darwin Trust of Edinburgh
- National Institutes of Health (1s10od016212-01)
- National Institute of General Medical Sciences (S10-OD016212, R35GM119455)
- 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 › Molecular Biology › DNA Repair Mechanisms
- Keywords
- mitosis
- MeSH terms
- Centromere, Humans, Meiosis, Mitosis, CDC2 Protein Kinase, Cell Cycle Proteins, Protein Phosphatase 2
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