ArticleBiology of reproduction2008
UBE2I (UBC9), a SUMO-conjugating enzyme, localizes to nuclear speckles and stimulates transcription in mouse oocytes.
Article in Biology of reproduction, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
42 citing papers in PubMed, 65 citations in OpenAlex.
- Molecular mechanisms of folliculogenesis and oogenesis.Systems biology in reproductive medicine · 2026Review
- U2AF1 modulates alternative exon selection and guards zygotic splicing activation in mouse preimplantation embryogenesis.Cellular and molecular life sciences : CMLS · 2026Article
- Natural degradation of RNA polymerase II is essential for oocyte chromatin reorganization and maternal-to-zygotic transition.Nature communications · 2025Article
- Review
- Disruption of oocyte SUMOylation impacts critical regulatory processes during folliculogenesis in mice†.Biology of reproduction · 2025Article
- Article
- SUMO2/3 conjugation of TDP-43 protects against aggregation.Science advances · 2025Article
- The Chronic Toxicity of Endocrine-Disrupting Chemical toInternational journal of molecular sciences · 2024Article
- An adaptive stress response that confers cellular resilience to decreased ubiquitination.Nature communications · 2023Article
- Paradoxes of Cellular SUMOylation Regulation: A Role of Biomolecular Condensates?Pharmacological reviews · 2023Review
- Transcriptomics and the origin of obligate parthenogenesis.Heredity · 2023Article
- Regulation of Pre-mRNA Splicing: Indispensable Role of Post-Translational Modifications of Splicing Factors.Life (Basel, Switzerland) · 2023Review
- Regulation of SUMOylation on RNA metabolism in cancers.Frontiers in molecular biosciences · 2023Review
- SUMO conjugation regulates the activity of the Integrator complex.Nucleic acids research · 2022Article
- Promyelocytic leukemia nuclear body-like structures can assemble in mouse oocytes.Biology open · 2022Article
- Keeping up with the condensates: The retention, gain, and loss of nuclear membrane-less organelles.Frontiers in molecular biosciences · 2022Review
- Ubiquitination and Ubiquitin-Like Modifications as Mediators of Alternative Pre-mRNA Splicing inFrontiers in plant science · 2022Review
- Mechanisms of Oocyte Maturation and Related Epigenetic Regulation.Frontiers in cell and developmental biology · 2021Review
- Transcriptomic analyses suggest that mucopolysaccharidosis patients may be less susceptible to COVID-19.FEBS letters · 2020Article
- Isoforsythiaside Attenuates Alzheimer's Disease via Regulating Mitochondrial Function Through the PI3K/AKT Pathway.International journal of molecular sciences · 2020Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Sumoylation is a posttranslational modification in which SUMO (small ubiquitin-related modifier) proteins are covalently attached to their substrates. In vertebrates, developmental roles for sumoylation have been studied, but the function of sumoylation during mammalian oocyte growth and maturation is not known. As a prelude to conducting studies on the role of sumoylation during oocyte development, we analyzed the temporal and spatial pattern of expression of UBE2I, a SUMO-conjugating E2 enzyme. Immunocytochemical analysis of UBE2I revealed a punctate nuclear staining pattern, with transcriptionally quiescent, fully grown, GV-intact oocytes having larger UBE2I-containing bodies than transcriptionally active, meiotically incompetent growing oocytes. Inhibiting transcription in incompetent oocytes resulted in an increase in the size of the UBE2I-containing bodies. Overexpression of either wild-type UBE2I or catalytically inactive UBE2I resulted in an increase in the size of the UBE2I-containing bodies but also an increase in BrUTP incorporation, suggesting that transcriptional activation by UBE2I is independent of its catalytic activity. Although UBE2I-containing bodies did not completely colocalize with SUMO1 or SUMO2 and SUMO3, which were localized mainly on the nuclear membrane and in the nucleoplasm, UBE2I strikingly colocalized with SFRS2, which is a component of nuclear speckles and critical for mRNA processing. These results suggest a novel function for UBE2I and therefore sumoylation in gene expression.
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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.