ArticleThe Journal of biological chemistry2015
The MLLE domain of the ubiquitin ligase UBR5 binds to its catalytic domain to regulate substrate binding.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 44 citations in OpenAlex.
- Article
- Deciphering the RNA-binding protein network during endosomal mRNA transport.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- 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
- Large-scale phage-based screening reveals extensive pan-viral mimicry of host short linear motifs.Nature communications · 2023Article
- Article
- Ubiquitin-modifying enzymes in Huntington's disease.Frontiers in molecular biosciences · 2023Review
- A MademoiseLLE domain binding platform links the key RNA transporter to endosomes.PLoS genetics · 2022Article
- Role of ubiquitin-protein ligase UBR5 in the disassembly of mitotic checkpoint complexes.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- UBR5 promotes tumor immune evasion through enhancing IFN-γ-inducedTheranostics · 2022Article
- LARP1 and LARP4: up close with PABP for mRNA 3' poly(A) protection and stabilization.RNA biology · 2021Review
- How to Inactivate Human Ubiquitin E3 Ligases by Mutation.Frontiers in cell and developmental biology · 2020Review
- Characterization of interaction and ubiquitination of phosphoenolpyruvate carboxykinase by E3 ligase UBR5.Biology open · 2018Article
- The E3 ubiquitin ligase UBR5 regulates centriolar satellite stability and primary cilia.Molecular biology of the cell · 2018Article
- Wnt-Dependent Inactivation of the Groucho/TLE Co-repressor by the HECT E3 Ubiquitin Ligase Hyd/UBR5.Molecular cell · 2017Article
- Article
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4 authors at 1 institution in 1 country.
Funding
Abstract
E3 ubiquitin ligases catalyze the transfer of ubiquitin from an E2-conjugating enzyme to a substrate. UBR5, homologous to the E6AP C terminus (HECT)-type E3 ligase, mediates the ubiquitination of proteins involved in translation regulation, DNA damage response, and gluconeogenesis. In addition, UBR5 functions in a ligase-independent manner by prompting protein/protein interactions without ubiquitination of the binding partner. Despite recent functional studies, the mechanisms involved in substrate recognition and selective ubiquitination of its binding partners remain elusive. The C terminus of UBR5 harbors the HECT catalytic domain and an adjacent MLLE domain. MLLE domains mediate protein/protein interactions through the binding of a conserved peptide motif, termed PAM2. Here, we characterize the binding properties of the UBR5 MLLE domain to PAM2 peptides from Paip1 and GW182. The crystal structure with a Paip1 PAM2 peptide reveals the network of hydrophobic and ionic interactions that drive binding. In addition, we identify a novel interaction of the MLLE domain with the adjacent HECT domain mediated by a PAM2-like sequence. Our results confirm the role of the MLLE domain of UBR5 in substrate recruitment and suggest a potential role in regulating UBR5 ligase activity.
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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.