ArticleThe Journal of biological chemistry2016
Degradation of the Separase-cleaved Rec8, a Meiotic Cohesin Subunit, by the N-end Rule Pathway.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 26 citations in OpenAlex.
- Testicular fat deposition attenuates reproductive performance via decreased follicle-stimulating hormone level and sperm meiosis and testosterone synthesis in mouse.Animal bioscience · 2024Article
- A high level of the long non-coding RNABioengineered · 2022Article
- How the ends signal the end: Regulation by E3 ubiquitin ligases recognizing protein termini.Molecular cell · 2022Review
- Article
- Low tolerance for transcriptional variation at cohesin genes is accompanied by functional links to disease-relevant pathways.Journal of medical genetics · 2021Article
- Tex19.1 inhibits the N-end rule pathway and maintains acetylated SMC3 cohesin and sister chromatid cohesion in oocytes.The Journal of cell biology · 2020Article
- FBXO47 regulates telomere-inner nuclear envelope integration by stabilizing TRF2 during meiosis.Nucleic acids research · 2019Article
- Article
- Tex19.1 promotes Spo11-dependent meiotic recombination in mouse spermatocytes.PLoS genetics · 2017Article
- H2B ubiquitination regulates meiotic recombination by promoting chromatin relaxation.Nucleic acids research · 2016Article
- Phosphorylation Impacts N-end Rule Degradation of the Proteolytically Activated Form of BMX Kinase.The Journal of biological chemistry · 2016Article
- Analyzing N-terminal Arginylation through the Use of Peptide Arrays and Degradation Assays.The Journal of biological chemistry · 2016Article
- Article
- Physiological functions and clinical implications of the N-end rule pathway.Frontiers of medicine · 2016Review
- Protein arginylation regulates cellular stress response by stabilizing HSP70 and HSP40 transcripts.Cell death discoveryArticle
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Authors and funding
14 authors at 6 institutions in 2 countries.
Funding
Abstract
The Ate1 arginyltransferase (R-transferase) is a component of the N-end rule pathway, which recognizes proteins containing N-terminal degradation signals called N-degrons, polyubiquitylates these proteins, and thereby causes their degradation by the proteasome. Ate1 arginylates N-terminal Asp, Glu, or (oxidized) Cys. The resulting N-terminal Arg is recognized by ubiquitin ligases of the N-end rule pathway. In the yeastSaccharomyces cerevisiae, the separase-mediated cleavage of the Scc1/Rad21/Mcd1 cohesin subunit generates a C-terminal fragment that bears N-terminal Arg and is destroyed by the N-end rule pathway without a requirement for arginylation. In contrast, the separase-mediated cleavage of Rec8, the mammalian meiotic cohesin subunit, yields a fragment bearing N-terminal Glu, a substrate of the Ate1 R-transferase. Here we constructed and used a germ cell-confinedAte1(-/-)mouse strain to analyze the separase-generated C-terminal fragment of Rec8. We show that this fragment is a short-lived N-end rule substrate, that its degradation requires N-terminal arginylation, and that maleAte1(-/-)mice are nearly infertile, due to massive apoptotic death ofAte1(-/-)spermatocytes during the metaphase of meiosis I. These effects ofAte1ablation are inferred to be caused, at least in part, by the failure to destroy the C-terminal fragment of Rec8 in the absence of N-terminal arginylation.
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