The M-phase regulatory phosphatase PP2A-B55δ opposes protein kinase A on Arpp19 to initiate meiotic division

Tom Lemonnier, Enrico Maria Daldello, Robert Poulhe, Tran Le, Marika Miot, Laurent Lignières, Catherine Jessus and Aude Dupré ()
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Tom Lemonnier: Sorbonne Université, CNRS, Laboratoire de Biologie du Développement—Institut de Biologie Paris Seine, LBD—IBPS
Enrico Maria Daldello: Sorbonne Université, CNRS, Laboratoire de Biologie du Développement—Institut de Biologie Paris Seine, LBD—IBPS
Robert Poulhe: Sorbonne Université, CNRS, Laboratoire de Biologie du Développement—Institut de Biologie Paris Seine, LBD—IBPS
Tran Le: Sorbonne Université, CNRS, Laboratoire de Biologie du Développement—Institut de Biologie Paris Seine, LBD—IBPS
Marika Miot: Sorbonne Université, CNRS, Laboratoire de Biologie du Développement—Institut de Biologie Paris Seine, LBD—IBPS
Laurent Lignières: Université de Paris, CNRS, Institut Jacques Monod
Catherine Jessus: Sorbonne Université, CNRS, Laboratoire de Biologie du Développement—Institut de Biologie Paris Seine, LBD—IBPS
Aude Dupré: Sorbonne Université, CNRS, Laboratoire de Biologie du Développement—Institut de Biologie Paris Seine, LBD—IBPS

Nature Communications, 2021, vol. 12, issue 1, 1-16

Abstract: Abstract Oocytes are held in meiotic prophase for prolonged periods until hormonal signals trigger meiotic divisions. Key players of M-phase entry are the opposing Cdk1 kinase and PP2A-B55δ phosphatase. In Xenopus, the protein Arpp19, phosphorylated at serine 67 by Greatwall, plays an essential role in inhibiting PP2A-B55δ, promoting Cdk1 activation. Furthermore, Arpp19 has an earlier role in maintaining the prophase arrest through a second serine (S109) phosphorylated by PKA. Prophase release, induced by progesterone, relies on Arpp19 dephosphorylation at S109, owing to an unknown phosphatase. Here, we identified this phosphatase as PP2A-B55δ. In prophase, PKA and PP2A-B55δ are simultaneously active, suggesting the presence of other important targets for both enzymes. The drop in PKA activity induced by progesterone enables PP2A-B55δ to dephosphorylate S109, unlocking the prophase block. Hence, PP2A-B55δ acts critically on Arpp19 on two distinct sites, opposing PKA and Greatwall to orchestrate the prophase release and M-phase entry.

Date: 2021
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-22124-0

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DOI: 10.1038/s41467-021-22124-0

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