ArticleProceedings of the National Academy of Sciences of the United States of America2007
Mechanism of degradation of CPEB during Xenopus oocyte maturation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed, 84 citations in OpenAlex.
- Role of CPEBs in Learning and Memory.Journal of neurochemistry · 2025Review
- Translational repression by 4E-T is crucial to maintain the prophase-I arrest in vertebrate oocytes.Nature communications · 2025Article
- Decoding protein phosphorylation during oocyte meiotic divisions using phosphoproteomics.eLife · 2025Article
- Multiple intersecting pathways are involved in CPEB1 phosphorylation and regulation of translation during mouse oocyte meiosis.Development (Cambridge, England) · 2024Article
- Article
- A genome-wide perspective of the maternal mRNA translation program during oocyte development.Seminars in cell & developmental biology · 2024Review
- Multiple intersecting pathways are involved in the phosphorylation of CPEB1 to activate translation during mouse oocyte meiosis.bioRxiv : the preprint server for biology · 2024Article
- On-capillary alkylation micro-reactor: a facile strategy for proteo-metabolome profiling in the same single cells.Chemical science · 2023Article
- CPEB and translational control by cytoplasmic polyadenylation: impact on synaptic plasticity, learning, and memory.Molecular psychiatry · 2023Review
- Cytoplasmic Polyadenylation Is an Ancestral Hallmark of Early Development in Animals.Molecular biology and evolution · 2023Article
- Comparative analyses of vertebrate CPEB proteins define two subfamilies with coordinated yet distinct functions in post-transcriptional gene regulation.Genome biology · 2022Article
- Ultrasensitive Ribo-seq reveals translational landscapes during mammalian oocyte-to-embryo transition and pre-implantation development.Nature cell biology · 2022Article
- Review
- Aurora kinase B inhibits aurora kinase A to control maternal mRNA translation in mouse oocytes.Development (Cambridge, England) · 2021Article
- Oocyte meiosis-coupled poly(A) polymerase α phosphorylation and activation trigger maternal mRNA translation in mice.Nucleic acids research · 2021Article
- The Recurrent Mutation in PATL2 Inhibits Its Degradation Thus Causing Female Infertility Characterized by Oocyte Maturation Defect Through Regulation of the Mos-MAPK Pathway.Frontiers in cell and developmental biology · 2021Article
- The neglected part of early embryonic development: maternal protein degradation.Cellular and molecular life sciences : CMLS · 2020Review
- Translational Control ofCells · 2020Review
- Positive Feedback Stimulation ofFrontiers in cell and developmental biology · 2020Article
- SCFβ-TrCP ubiquitinates CHK1 in an AMPK-dependent manner in response to glucose deprivation.Molecular oncology · 2019Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
CPEB, a cytoplasmic polyadenylation element-binding protein, plays an important role in translational control of maternal mRNAs in early animal development. During Xenopus oocyte maturation, CPEB undergoes a Cdc2-mediated phosphorylation- and ubiquitin-dependent degradation that is required for proper entry into meiosis II. However, the precise mechanism of CPEB degradation, including the identity of the responsible E3 ubiquitin ligase, is not known. Here, we show that the SCF(beta-TrCP) E3 ubiquitin ligase complex targets CPEB for degradation during Xenopus oocyte maturation. beta-TrCP, the F-box protein of SCF(beta-TrCP), specifically binds to a sequence (190)TSGFSS(195) (termed here the TSG motif) of CPEB, thereby targeting CPEB for degradation. beta-TrCP binding depends on phosphorylation of Thr-190, Ser-191, and Ser-195 in the TSG motif. Among these residues, Ser-191 is phosphorylated by the Polo-like kinase Plx1, which binds CPEB at a specific Thr-125 residue prephosphorylated by Cdc2. Finally, Cdc2-mediated phosphorylation of other multiple Ser residues, previously implicated in CPEB degradation, is required for both Thr-125 phosphorylation and beta-TrCP binding, presumably causing conformational changes of CPEB. We propose that Cdc2 and Plx1 sequentially phosphorylate CPEB and target it for SCF(beta-TrCP)-dependent degradation in Xenopus oocytes. We suggest that many other proteins carrying the TSG-like motif may be targeted by SCF(beta-TrCP).
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