ArticleThe Journal of biological chemistry2019
Structural insights into non-covalent ubiquitin activation of the cIAP1-UbcH5B∼ubiquitin complex.
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 15 papers.
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Who cites it
15 citing papers in PubMed, 21 citations in OpenAlex.
- Structural basis for E4 enzyme Ufd2-catalyzed K48/K29 branched ubiquitin chains.Nature chemical biology · 2026Article
- Tuning ubiquitin transfer by RING E3 ubiquitin ligases through the linchpin residue.Life science alliance · 2025Article
- Article
- Mechanism of nucleosomal H2A K13/15 monoubiquitination and adjacent dual monoubiquitination by RNF168.Nature chemical biology · 2025Article
- Chemical Tools for Probing the Ub/Ubl Conjugation Cascades.Chembiochem : a European journal of chemical biology · 2025Review
- Mechanisms of RNF168 nucleosome recognition and ubiquitylation.Molecular cell · 2024Article
- Multisite phosphorylation dictates selective E2-E3 pairing as revealed by Ubc8/UBE2H-GID/CTLH assemblies.Molecular cell · 2024Article
- Article
- A non-canonical scaffold-type E3 ligase complex mediates protein UFMylation.The EMBO journal · 2022Article
- Unveiling the Essential Role of Arkadia's Non-RING Elements in the Ubiquitination Process.International journal of molecular sciences · 2022Article
- Ubiquitin and a charged loop regulate the ubiquitin E3 ligase activity of Ark2C.Nature communications · 2022Article
- Structural basis for the E3 ligase activity enhancement of yeast Nse2 by SUMO-interacting motifs.Nature communications · 2021Article
- Structural basis of generic versus specific E2-RING E3 interactions in protein ubiquitination.Protein science : a publication of the Protein Society · 2019Review
- Protein engineering of a ubiquitin-variant inhibitor of APC/C identifies a cryptic K48 ubiquitin chain binding site.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Structural insights into E1 recognition and the ubiquitin-conjugating activity of the E2 enzyme Cdc34.Nature communications · 2019Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Ubiquitin (Ub)-conjugating enzymes and Ub ligases control protein degradation and regulate many cellular processes in eukaryotes. Cellular inhibitor of apoptosis protein-1 (cIAP1) plays a central role in apoptosis and tumor necrosis factor signaling. It harbors a C-terminal RING domain that homodimerizes to recruit E2∼Ub (where ∼ denotes a thioester bond) complex to catalyze Ub transfer. Noncovalent Ub binding to the backside of the E2 Ub-conjugating enzyme UbcH5 has previously been shown to enhance RING domain activity, but the molecular basis for this enhancement is unclear. To investigate how dimeric cIAP1 RING activates E2∼Ub for Ub transfer and what role noncovalently bound Ub has in Ub transfer, here we determined the crystal structure of the cIAP1 RING dimer bound to both UbcH5B covalently linked to Ub (UbcH5B-Ub) and a noncovalent Ub to 1.7 Å resolution. The structure along with biochemical analyses revealed that the cIAP1 RING domain interacts with UbcH5B-Ub and thereby promotes the formation of a closed UbcH5B-Ub conformation that primes the thioester bond for Ub transfer. We observed that the noncovalent Ub binds to the backside of UbcH5B and abuts UbcH5B's α1β1-loop, which, in turn, stabilizes the closed UbcH5B-Ub conformation. Our results disclose the mechanism by which cIAP1 RING dimer activates UbcH5B∼Ub and indicate that noncovalent Ub binding further stabilizes the cIAP1-UbcH5B∼Ub complex in the active conformation to stimulate Ub transfer.
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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.