ArticleProceedings of the National Academy of Sciences of the United States of America2003
RFPL4 interacts with oocyte proteins of the ubiquitin-proteasome degradation pathway.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 75 citations in OpenAlex.
- The degradation of maternal RNA-binding protein 4E-T regulates translational activation to ensure maternal-to-zygotic transition in mouse embryos.Cellular and molecular life sciences : CMLS · 2026Article
- The timing of maternal protein degradation during mammalian preimplantation development is species-specific.Reproduction (Cambridge, England) · 2025Article
- The E3 ubiquitin ligase adaptor KLHL8 targets ZAR1 to regulate maternal mRNA degradation in oocytes.EMBO reports · 2025Article
- Heterozygous Eif4nif1 Stop-Gain Mice Replicate the Primary Ovarian Insufficiency Phenotype in Women.Endocrinology · 2025Article
- Review
- Genetic basis of maize maternal haploid induction beyondFrontiers in plant science · 2023Article
- The requirement of ubiquitin C-terminal hydrolase L1 in mouse ovarian development and fertility†.Biology of reproduction · 2022Article
- The Conceivable Functions of Protein Ubiquitination and Deubiquitination in Reproduction.Frontiers in physiology · 2022Review
- Extracellular vesicles and female reproduction.Journal of assisted reproduction and genetics · 2021Review
- The neglected part of early embryonic development: maternal protein degradation.Cellular and molecular life sciences : CMLS · 2020Review
- The role of SCF ubiquitin-ligase complex at the beginning of life.Reproductive biology and endocrinology : RB&E · 2019Review
- Fbxo30 regulates chromosome segregation of oocyte meiosis.Cellular and molecular life sciences : CMLS · 2019Article
- Post-translational regulation of the maternal-to-zygotic transition.Cellular and molecular life sciences : CMLS · 2018Review
- ACCERBATIN, a small molecule at the intersection of auxin and reactive oxygen species homeostasis with herbicidal properties.Journal of experimental botany · 2017Article
- Article
- Autophagic activity as an indicator for selecting good quality embryos.Reproductive medicine and biology · 2015Review
- RFPL4A increases the G1 population and decreases sensitivity to chemotherapy in human colorectal cancer cells.The Journal of biological chemistry · 2015Article
- Article
- Article
- Structure and function of the SPRY/B30.2 domain proteins involved in innate immunity.Protein science : a publication of the Protein Society · 2013Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Oocyte meiosis and early mitotic divisions in developing embryos rely on the timely production of cell cycle regulators and their clearance via proteasomal degradation. Ret Finger Protein-Like 4 (Rfpl4), encoding a RING finger-like protein with a B30.2 domain, was discovered during an in silico search for germ cell-specific genes. To study the expression and functions of RFPL4 protein, we performed immunolocalizations and used yeast two-hybrid and other protein-protein interaction assays. Immunohistochemistry and immunofluorescence showed that RFPL4 accumulates in all growing oocytes and quickly disappears during early embryonic cleavage. We used a yeast two-hybrid model to demonstrate that RFPL4 interacts with the E2 ubiquitin-conjugating enzyme HR6A, proteasome subunit beta type 1, ubiquitin B, as well as a degradation target protein, cyclin B1. Coimmunoprecipitation analyses of in vitro translated proteins and extracts of transiently cotransfected Chinese hamster ovary (CHO)-K1 cells confirmed these findings. We conclude that, like many RING-finger containing proteins, RFPL4 is an E3 ubiquitin ligase. The specificity of its expression and these interactions suggest that RFPL4 targets cyclin B1 for proteasomal degradation, a key aspect of oocyte cell cycle control during meiosis and the crucial oocyte-to-embryo transition to mitosis.
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