IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v12y2021i1d10.1038_s41467-021-22124-0.html
   My bibliography  Save this article

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

Author

Listed:
  • 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)

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.

Suggested Citation

  • Tom Lemonnier & Enrico Maria Daldello & Robert Poulhe & Tran Le & Marika Miot & Laurent Lignières & Catherine Jessus & Aude Dupré, 2021. "The M-phase regulatory phosphatase PP2A-B55δ opposes protein kinase A on Arpp19 to initiate meiotic division," Nature Communications, Nature, vol. 12(1), pages 1-16, December.
    • Handle: RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-22124-0
    DOI: 10.1038/s41467-021-22124-0
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-021-22124-0
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/s41467-021-22124-0?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-22124-0. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    We have no bibliographic references for this item. You can help adding them by using this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.