Journal
JOURNAL OF CELL BIOLOGY
Volume 217, Issue 12, Pages 4106-4123Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.201804018
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Funding
- Canadian Institutes of Health Research [MOP-133558]
- Natural Sciences and Engineering Research Council of Canada [402217-2011 RGP IN, RGP IN-2017-05839]
- Fonds de Recherche du Quebec - Sante
- Canada Foundation for Innovation
- Fonds de Fecherche du Quebec - Sante
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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 maternaleffect 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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