ArticleThe Journal of biological chemistry2019
Coupled monoubiquitylation of the co-E3 ligase DCNL1 by Ariadne-RBR E3 ubiquitin ligases promotes cullin-RING ligase complex remodeling.
Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 18 citations in OpenAlex.
- E3 ubiquitin ligases: structural diversity, dysregulation in disease, and their emerging role in targeted therapeutic strategies.Frontiers in molecular biosciences · 2026Review
- HOIL-1 ubiquitin ligase activity targets unbranched glucosaccharides and is required to prevent polyglucosan accumulation.The EMBO journal · 2022Article
- Co-adaptor driven assembly of a CUL3 E3 ligase complex.Molecular cell · 2022Article
- The roles of E3 ligases in Hepatocellular carcinoma.American journal of cancer research · 2022Review
- The ubiquitin ligation machinery in the defense against bacterial pathogens.EMBO reports · 2021Review
- Functional roles of E3 ubiquitin ligases in gastric cancer.Oncology letters · 2020Review
- Chain reactions: molecular mechanisms of RBR ubiquitin ligases.Biochemical Society transactions · 2020Review
- Haplotype-resolved genomes provide insights into structural variation and gene content in Angus and Brahman cattle.Nature communications · 2020Article
- In Vitro Reconstitution Defines the Minimal Requirements for Cdc48-Dependent Disassembly of the CMG Helicase in Budding Yeast.Cell reports · 2019Article
- The E3 ligase HOIL-1 catalyses ester bond formation between ubiquitin and components of the Myddosome in mammalian cells.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Cullin-RING E3 ubiquitin ligases (CRLs) are large and diverse multisubunit protein complexes that contribute to about one-fifth of ubiquitin-dependent protein turnover in cells. CRLs are activated by the attachment of the ubiquitin-like protein neural precursor cell expressed, developmentally down-regulated 8 (NEDD8) to the cullin subunits. This cullin neddylation is essential for a plethora of CRL-regulated cellular processes and is vital for life. In mammals, neddylation is promoted by the five co-E3 ligases, defective in cullin neddylation 1 domain-containing 1-5 (DCNL1-5); however, their functional regulation within the CRL complex remains elusive. We found here that the ubiquitin-associated (UBA) domain-containing DCNL1 is monoubiquitylated when bound to CRLs and that this monoubiquitylation depends on the CRL-associated Ariadne RBR ligases TRIAD1 (ARIH2) and HHARI (ARIH1) and strictly requires the DCNL1's UBA domain. Reconstitution of DCNL1 monoubiquitylation
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