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- W3136558119 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." @default.
- W3136558119 created "2021-03-29" @default.
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- W3136558119 date "2021-03-23" @default.
- W3136558119 modified "2023-10-17" @default.
- W3136558119 title "The M-phase regulatory phosphatase PP2A-B55δ opposes protein kinase A on Arpp19 to initiate meiotic division" @default.
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- W3136558119 doi "https://doi.org/10.1038/s41467-021-22124-0" @default.
- W3136558119 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/7988065" @default.
- W3136558119 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/33758202" @default.
- W3136558119 hasPublicationYear "2021" @default.
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