ArticleGenes2010
Evidence Implicating CCNB1IP1, a RING Domain-Containing Protein Required for Meiotic Crossing Over in Mice, as an E3 SUMO Ligase.
Article in Genes, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
What it found
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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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
23 citing papers in PubMed, 31 citations in OpenAlex.
- Crossover formation and coordinated assembly of synaptonemal complex relies on a direct interaction between Zip1 and Zip3.Genetics · 2026Article
- Molecular architecture of meiotic pro-crossover factor HEI10 reveals coupling of higher-order assembly and ubiquitin chain formation.bioRxiv : the preprint server for biology · 2026Article
- Article
- Crossover formation and coordinated assembly of synaptonemal complex relies on a direct interaction between Zip1 and Zip3.bioRxiv : the preprint server for biology · 2025Article
- Article
- Chromosome architecture and homologous recombination in meiosis.Frontiers in cell and developmental biology · 2022Review
- Ubiquitination in Plant Meiosis: Recent Advances and High Throughput Methods.Frontiers in plant science · 2021Review
- Expression of Ralstonia solanacearum type III secretion system is dependent on a novel type 4 pili (T4P) assembly protein (TapV) but is T4P independent.Molecular plant pathology · 2020Article
- Review
- Narya, a RING finger domain-containing protein, is required for meiotic DNA double-strand break formation and crossover maturation in Drosophila melanogaster.PLoS genetics · 2019Article
- HEIP1 regulates crossover formation during meiosis in rice.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Ccdc181 is a microtubule-binding protein that interacts with Hook1 in haploid male germ cells and localizes to the sperm tail and motile cilia.European journal of cell biology · 2017Article
- Control of Meiotic Crossovers: From Double-Strand Break Formation to Designation.Annual review of genetics · 2016Review
- Sexually Dimorphic Gene Expression Associated with Growth and Reproduction of Tongue Sole (Cynoglossus semilaevis) Revealed by Brain Transcriptome Analysis.International journal of molecular sciences · 2016Article
- Article
- A novel derivative of betulinic acid, SYK023, suppresses lung cancer growth and malignancy.Oncotarget · 2015Article
- Mammalian CNTD1 is critical for meiotic crossover maturation and deselection of excess precrossover sites.The Journal of cell biology · 2014Article
- E3 ligase Hei10: a multifaceted structure-based signaling molecule with roles within and beyond meiosis.Genes & development · 2014Article
- Antagonistic roles of ubiquitin ligase HEI10 and SUMO ligase RNF212 regulate meiotic recombination.Nature genetics · 2014Article
- RNF212 is a dosage-sensitive regulator of crossing-over during mammalian meiosis.Nature genetics · 2013Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The RING domain-containing protein CCNB1IP1 (Cyclin B1 Interacting Protein 1) is a putative ubiquitin E3 ligase that is essential for chiasmata formation, and hence fertility, in mice. Previous studies in cultured cells indicated that CCNB1IP1 targets Cyclin B for degradation, thus playing a role in cell cycle regulation. Mice homozygous for a mutant allele (mei4) of Ccnb1ip1 display no detectable phenotype other than meiotic failure from an absence of chiasmata. CCNB1IP1 is not conserved in key model organisms such as yeast and Drosophila, and there are no features of the protein that implicate clear mechanisms for a role in recombination. To gain insight into CCNB1IP1's function in meiotic cells, we raised a specific antibody and determined that the protein appears in pachynema. This indicates that CCNB1IP1 is involved with crossover intermediate maturation, rather than early (leptotene) specification of a subset of SPO11-induced double strand breaks towards the crossover pathway. Additionally, a yeast 2-hybrid (Y2H) screen revealed that CCNB1IP1 interacts with SUMO2 and a set of proteins enriched for consensus sumoylation sites. The Y2H studies, combined with scrutiny of CCNB1IP1 domains, implicate this protein as an E3 ligase of the sumoylation cascade. We hypothesize CCNB1IP1 represents a novel meiosis-specific SUMO E3 ligase critical to resolution of recombination intermediates into mature chiasmata.
Identifiers
What OpenQuestion holds
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.