ArticleMolecules and cells2013
Cdc25B phosphatase participates in maintaining metaphase II arrest in mouse oocytes.
Article in Molecules and cells, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers, 1 of them a synthesis that pooled it.
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Who cites it
8 citing papers in PubMed, 1 synthesis or guideline pooled it, 18 citations in OpenAlex.
- Platelet-rich plasma and folliculogenesis: a systematic mechanistic review and computational pathway analysis.Frontiers in reproductive health · 2026Pooled it
- Genetic Diversity, Admixture, and Selection Signatures in a Rarámuri Criollo Cattle Population Introduced to the Southwestern United States.International journal of molecular sciences · 2025Article
- Genome-Wide Population Structure and Selection Signatures of Yunling Goat Based on RAD-seq.Animals : an open access journal from MDPI · 2022Article
- Sarcoma-180 tumor affects the quality of oocytes in mice.Oncology letters · 2021Article
- Luteinizing Hormone Action in Human Oocyte Maturation and Quality: Signaling Pathways, Regulation, and Clinical Impact.Reproductive sciences (Thousand Oaks, Calif.) · 2020Review
- Involvement of CaMKII in regulating the release of diplotene-arrested mouse oocytes by pAkt1 (Ser473).Cell cycle (Georgetown, Tex.) · 2019Article
- Calcium influx and sperm-evoked calcium responses during oocyte maturation and egg activation.Oncotarget · 2017Review
- Molecular determinants of the meiotic arrests in mammalian oocytes at different stages of maturation.Cell cycle (Georgetown, Tex.)Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cdc25B is an essential regulator for meiotic resumption in mouse oocytes. However, the role of this phosphatase during the later stage of the meiotic cell cycle is not known. In this study, we investigated the role of Cdc25B during metaphase II (MII) arrest in mouse oocytes. Cdc25B was extensively phosphorylated during MII arrest with an increase in the phosphatase activity toward Cdk1. Downregulation of Cdc25B by antibody injection induced the formation of a pronucleus-like structure. Conversely, overexpression of Cdc25B inhibited Ca(2+)-mediated release from MII arrest. Moreover, Cdc25B was immediately dephosphorylated and hence inactivated during MII exit, suggesting that Cdk1 phosphorylation is required to exit from MII arrest. Interestingly, this inactivation occurred prior to cyclin B degradation. Taken together, our data demonstrate that MII arrest in mouse oocytes is tightly regulated not only by the proteolytic degradation of cyclin B but also by dynamic phosphorylation of Cdk1.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.