PP2A-B55 promotes nuclear envelope reformation after mitosis in Drosophila
Open accessAbstract
As a dividing cell exits mitosis and daughter cells enter interphase, many proteins must be dephosphorylated. The protein phosphatase 2A (PP2A) with its B55 regulatory subunit plays a crucial role in this transition, but the identity of its substrates and how their dephosphorylation promotes mitotic exit are largely unknown. We conducted a maternal-effect screen in Drosophila melanogaster to identify genes that function with PP2A-B55/Tws in the cell cycle. We found that eggs that receive reduced levels of Tws and of components of the nuclear envelope (NE) often fail development, concomitant with NE defects following meiosis and in syncytial mitoses. Our mechanistic studies using Drosophila cells indicate that PP2A-Tws promotes nuclear envelope reformation (NER) during mitotic exit by dephosphorylating BAF and suggests that PP2A-Tws targets additional NE components, including Lamin and Nup107. This work establishes Drosophila as a powerful model to further dissect the molecular mechanisms of NER and suggests additional roles of PP2A-Tws in the completion of meiosis and mitosis.
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Dephosphorylation of selected substrates drives chromosome decondensation, nuclear envelope reformation, mitotic exit and cytokinesis.
“As a result, dephosphorylation of specific substrates drives orderly events including chromosome decondensation and nuclear envelope reformation, leading to proper mitotic exit and cytokinesis (Cundell et al., 2016; Mehsen et al., 2018).”
From PP2A holoenzymes, substrate specificity driving cellular functions and deregulation in cancer (2019) · cites this paper as Mehsen et al., 2018
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PP2A holoenzymes, substrate specificity driving cellular functions and deregulation in cancer
(2019) · Advances in Cancer Research · doi:10.1016/bs.acr.2019.03.009 · Cited by 93 · see citing works
- Authors
- Mehsen, H., Boudreau, V., Garrido, D., Bourouh, M., Larouche, M., Maddox, P. S., Swan, A., & Archambault, V.
- Affiliations
- Institute for Research in Immunology and Cancer (CA)
- University of Windsor (CA)
- Corresponding author
- Archambault, Vincent
- ORCID
- Venue
- Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2018-10-11
- Volume
- 217
- Issue
- 12
- Pages
- 4106-4123
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- PMC
- PMC6279390
- OpenAlex
- W2896537027
- Cited by
- 52
- References
- 61
- Citations by year
- 2026: 5 · 2025: 4 · 2024: 10 · 2023: 7 · 2022: 8 · 2021: 5 · 2020: 8 · 2019: 4 · 2018: 1
- FWCI
- 1.60
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- The Journal of Cell Biology (publishedVersion, cc-by-nc-sa)
- Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- Funders
- Canadian Institutes of Health Research (MOP-133558)
- Natural Sciences and Engineering Research Council of Canada (402217-2011 RGPIN, RGPIN 2017-05839)
- Fonds de Recherche du Québec – Santé
- Canada Foundation for Innovation
- Fonds de Fecherche du Québec – Santé
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
- 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
- Keywords
- PP2A-B55, protein phosphatase 2A, nuclear envelope reformation, mitotic exit, dephosphorylation, BAF, nuclear lamins, Nup107, meiosis, Drosophila melanogaster
- MeSH terms
- Animals, DNA-Binding Proteins, Drosophila melanogaster, Mitosis, Models, Biological, Nuclear Envelope, Nuclear Proteins, Phosphoprotein Phosphatases, Aquaporins, Drosophila Proteins, Lamins
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