ArticleActa crystallographica. Section F, Structural biology and crystallization communications2012
Structure of the HECT C-lobe of the UBR5 E3 ubiquitin ligase.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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19 citing papers in PubMed.
- UBR5 regulates the progression of colorectal cancer cells through Snail-induced epithelial-mesenchymal transition.Genes & diseases · 2026Article
- E3 ubiquitin ligase UBR5 modulates circadian rhythm by facilitating the ubiquitination and degradation of the key clock transcription factor BMAL1.Acta pharmacologica Sinica · 2024Article
- Research advancements on the involvement of E3 ubiquitin ligase UBR5 in gastrointestinal cancers.Heliyon · 2024Review
- Structural snapshots along K48-linked ubiquitin chain formation by the HECT E3 UBR5.Nature chemical biology · 2024Article
- Cryo-EM structure of the chain-elongating E3 ubiquitin ligase UBR5.The EMBO journal · 2023Article
- UBR5 forms ligand-dependent complexes on chromatin to regulate nuclear hormone receptor stability.Molecular cell · 2023Article
- Structure of the human UBR5 E3 ubiquitin ligase.Structure (London, England : 1993) · 2023Article
- Emerging roles of the HECT E3 ubiquitin ligases in gastric cancer.Pathology oncology research : POR · 2023Review
- It's not just a phase; ubiquitination in cytosolic protein quality control.Biochemical Society transactions · 2021Review
- Identification of the HECT E3 ligase UBR5 as a regulator of MYC degradation using a CRISPR/Cas9 screen.Scientific reports · 2020Article
- UBR5 regulates proliferation and radiosensitivity in human laryngeal carcinoma via the p38/MAPK signaling pathway.Oncology reports · 2020Article
- An Angelman syndrome substitution in the HECT E3 ubiquitin ligase C-terminal Lobe of E6AP affects protein stability and activity.PloS one · 2020Article
- UBR5 interacts with the replication fork and protects DNA replication from DNA polymerase η toxicity.Nucleic acids research · 2019Article
- E3 ubiquitin ligases in B-cell malignancies.Cellular immunology · 2019Review
- Characterization of interaction and ubiquitination of phosphoenolpyruvate carboxykinase by E3 ligase UBR5.Biology open · 2018Article
- Selection and Characterization of a DNA Aptamer Specifically Targeting Human HECT Ubiquitin Ligase WWP1.International journal of molecular sciences · 2018Article
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- The MLLE domain of the ubiquitin ligase UBR5 binds to its catalytic domain to regulate substrate binding.The Journal of biological chemistry · 2015Article
- Article
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4 authors.
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Abstract
UBR5 ubiquitin ligase (also known as EDD, Rat100 or hHYD) is a member of the E3 protein family of HECT (homologous to E6-AP C-terminus) ligases as it contains a C-terminal HECT domain. In ubiquitination cascades involving E3s of the HECT class, ubiquitin is transferred from an associated E2 ubiquitin-conjugating enzyme to the acceptor cysteine of the HECT domain, which consists of structurally distinct N- and C-lobes connected by a flexible linker. Here, the high-resolution crystal structure of the C-lobe of the HECT domain of human UBR5 is presented. The structure reveals important features that are unique compared with other HECT domains. In particular, a distinct four-residue insert in the second helix elongates this helix, resulting in a strikingly different orientation of the preceding loop. This protruding loop is likely to contribute to specificity towards the E2 ubiquitin-conjugating enzyme UBCH4, which is an important functional partner of UBR5. Ubiquitination assays showed that the C-lobe of UBR5 is able to form a thioester-linked E3-ubiquitin complex, although it does not physically interact with UBCH4 in NMR experiments. This study contributes to a better understanding of UBR5 ubiquitination activity.
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