ArticleMolecular cell2010
Catalysis of lysine 48-specific ubiquitin chain assembly by residues in E2 and ubiquitin.
Article in Molecular cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.
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Who cites it
60 citing papers in PubMed, 90 citations in OpenAlex.
- The UBE2/E2 ubiquitin-conjugating enzyme family at the interface of tumor biology and antitumor immunity: mechanisms, biomarkers, and therapeutic opportunities.Frontiers in immunology · 2026Review
- A comparative study of the cryo-EM structures ofeLife · 2024Article
- From seeds to trees: how E2 enzymes grow ubiquitin chains.Biochemical Society transactions · 2023Review
- Current perspectives of ubiquitination and SUMOylation in abiotic stress tolerance in plants.Frontiers in plant science · 2022Review
- SCFEMBO reports · 2021Article
- The UBA domain of conjugating enzyme Ubc1/Ube2K facilitates assembly of K48/K63-branched ubiquitin chains.The EMBO journal · 2021Article
- Recruitment of Ubiquitin within an E2 Chain Elongation Complex.Biophysical journal · 2020Article
- Unanchored Ubiquitin Chains, Revisited.Frontiers in cell and developmental biology · 2020Review
- Ubiquitination is required for the initial removal of paternal organelles in C. elegans.Developmental biology · 2019Article
- 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
- Analysis of ubiquitin recognition by the HECT ligase E6AP provides insight into its linkage specificity.The Journal of biological chemistry · 2019Article
- The potato cyst nematode effector RHA1B is a ubiquitin ligase and uses two distinct mechanisms to suppress plant immune signaling.PLoS pathogens · 2019Article
- Article
- Active Site Gate Dynamics Modulate the Catalytic Activity of the Ubiquitination Enzyme E2-25K.Scientific reports · 2018Article
- Ubiquitin-like Protein Conjugation: Structures, Chemistry, and Mechanism.Chemical reviews · 2018Review
- Hydrophobic Patch of Ubiquitin is Important for its Optimal Activation by Ubiquitin Activating Enzyme E1.Analytical chemistry · 2017Article
- Article
- Mechanism and disease association of E2-conjugating enzymes: lessons from UBE2T and UBE2L3.The Biochemical journal · 2016Review
- WD40 domain of Apc1 is critical for the coactivator-induced allosteric transition that stimulates APC/C catalytic activity.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Protein ubiquitination is catalyzed by ubiquitin-conjugating enzymes (E2s) in collaboration with ubiquitin-protein ligases (E3s). This process depends on nucleophilic attack by a substrate lysine on a thioester bond linking the C terminus of ubiquitin to a cysteine in the E2 active site. Different E2 family members display specificity for lysines in distinct contexts. We addressed the mechanistic basis for this lysine selectivity in Ubc1, an E2 that catalyzes the ubiquitination of lysine 48 (K48) in ubiquitin, leading to the formation of K48-linked polyubiquitin chains. We identified a cluster of polar residues near the Ubc1 active site, as well as a residue in ubiquitin itself, that are required for catalysis of K48-specific ubiquitin ligation, but not for general activity toward other lysines. Our results suggest that the active site of Ubc1, as well as the surface of ubiquitin, contains specificity determinants that channel specific lysines to the central residues involved directly in catalysis.
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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.