ArticleThe Journal of biological chemistry2010
The yeast E4 ubiquitin ligase Ufd2 interacts with the ubiquitin-like domains of Rad23 and Dsk2 via a novel and distinct ubiquitin-like binding domain.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 49 citations in OpenAlex.
- Structural basis for E4 enzyme Ufd2-catalyzed K48/K29 branched ubiquitin chains.Nature chemical biology · 2026Article
- UBE4B Mediates Mitophagy via NIPSNAP1 Ubiquitination and NDP52 Recruitment.International journal of molecular sciences · 2026Article
- E4 ubiquitin ligase promotes mitofusin turnover and mitochondrial stress response.Molecular cell · 2023Article
- Lysine deserts prevent adventitious ubiquitylation of ubiquitin-proteasome components.Cellular and molecular life sciences : CMLS · 2023Article
- A heterotypic assembly mechanism regulates CHIP E3 ligase activity.The EMBO journal · 2022Article
- An integrated DNA and RNA variant detector identifies a highly conserved three base exon in theRNA biology · 2021Article
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- Structure, Dynamics and Function of the 26S Proteasome.Sub-cellular biochemistry · 2021Review
- Genome-wide analysis of the U-box E3 ubiquitin ligase enzyme gene family in tomato.Scientific reports · 2020Article
- The Proteasome and Its Network: Engineering for Adaptability.Cold Spring Harbor perspectives in biology · 2020Review
- Structure and Function of the 26S Proteasome.Annual review of biochemistry · 2018Review
- UFD-2 is an adaptor-assisted E3 ligase targeting unfolded proteins.Nature communications · 2018Article
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- Article
- Ufd2p synthesizes branched ubiquitin chains to promote the degradation of substrates modified with atypical chains.Nature communications · 2017Article
- Sumoylation, Phosphorylation, and Acetylation Fine-Tune the Turnover of Plant Immunity Components Mediated by Ubiquitination.Frontiers in plant science · 2017Review
- (1)H, (15)N, (13)C resonance assignments for Saccharomyces cerevisiae Rad23 UBL domain.Biomolecular NMR assignments · 2016Article
- Structures of Rpn1 T1:Rad23 and hRpn13:hPLIC2 Reveal Distinct Binding Mechanisms between Substrate Receptors and Shuttle Factors of the Proteasome.Structure (London, England : 1993) · 2016Article
- Emerging mechanistic insights into AAA complexes regulating proteasomal degradation.Biomolecules · 2014Review
- Article
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Proteins containing ubiquitin-like (UBL) and ubiquitin-associated (UBA) domains interact with various binding partners and function as hubs during ubiquitin-mediated protein degradation. A common interaction of the budding yeast UBL-UBA proteins Rad23 and Dsk2 with the E4 ubiquitin ligase Ufd2 has been described in endoplasmic reticulum-associated degradation among other pathways. The UBL domains of Rad23 and Dsk2 play a prominent role in this process by interacting with Ufd2 and different subunits of the 26 S proteasome. Here, we report crystal structures of Ufd2 in complex with the UBL domains of Rad23 and Dsk2. The N-terminal UBL-interacting region of Ufd2 exhibits a unique sequence pattern, which is distinct from any known ubiquitin- or UBL-binding domain identified so far. Residue-specific differences exist in the interactions of these UBL domains with Ufd2, which are coupled to subtle differences in their binding affinities. The molecular details of their differential interactions point to a role for adaptive evolution in shaping these interfaces.
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Registered trials
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.