ArticleCell cycle (Georgetown, Tex.)2010
Female infertility in PDE3A(-/-) mice: polo-like kinase 1 (Plk1) may be a target of protein kinase A (PKA) and involved in meiotic arrest of oocytes from PDE3A(-/-) mice.
Article in Cell cycle (Georgetown, Tex.), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 15 citations in OpenAlex.
- The Role of PDE3A in Cancer.ACS omega · 2026Review
- Multiple Roles of PLK1 in Mitosis and Meiosis.Cells · 2023Review
- Targeting Polo-like kinase in space and time during C. elegans meiosis.Cell cycle (Georgetown, Tex.) · 2021Review
- High cGMP and low PDE3A activity are associated with oocyte meiotic incompetence.Cell cycle (Georgetown, Tex.) · 2019Article
- RhoA-mediated FMNL1 regulates GM130 for actin assembly and phosphorylates MAPK for spindle formation in mouse oocyte meiosis.Cell cycle (Georgetown, Tex.) · 2015Article
- Cyclic nucleotide phosphodiesterases: important signaling modulators and therapeutic targets.Oral diseases · 2015Review
- Polo-like kinase is required for synaptonemal complex disassembly and phosphorylation in mouse spermatocytes.Journal of cell science · 2012Article
- Role of PDE3A in regulation of cell cycle progression in mouse vascular smooth muscle cells and oocytes: implications in cardiovascular diseases and infertility.Current opinion in pharmacology · 2011Review
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Mechanisms of cAMP/PKA-induced meiotic arrest in oocytes are not completely identified. In cultured, G2/M-arrested PDE3A(-/-) murine oocytes, elevated PKA activity was associated with inactivation of Cdc2 and Plk1, and inhibition of phosphorylation of histone H3 (S10) and of dephosphorylation of Cdc25B (S323) and Cdc2 (Thr14/Tyr15). In cultured WT oocytes, PKA activity was transiently reduced and then increased to that observed in PDE3A(-/-) oocytes; Cdc2 and Plk1 were activated, phosphorylation of histone H3 (S10) and dephosphorylation of Cdc25B (S323) and Cdc2 (Thr14/Tyr15) were observed. In WT oocytes, PKAc were rapidly translocated into nucleus, and then to the spindle apparatus, but in PDE3A(-/-) oocytes, PKAc remained in the cytosol. Plk1 was reactivated by incubation of PDE3A(-/-) oocytes with PKA inhibitor, Rp-cAMPS. PDE3A was co-localized with Plk1 in WT oocytes, and co-immunoprecipitated with Plk1 in WT ovary and Hela cells. PKAc phosphorylated rPlk1 and Hela cell Plk1 and inhibited Plk1 activity in vitro. Our results suggest that PKA-induced inhibition of Plk1 may be critical in oocyte meiotic arrest and female infertility in PDE3A(-/-) mice.
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