ArticleBiochemistry2014
The ubiquitin-conjugating enzyme, UbcM2, is restricted to monoubiquitylation by a two-fold mechanism that involves backside residues of E2 and Lys48 of ubiquitin.
Article in Biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- A nanobody that binds to the backside of the ubiquitin conjugating enzyme Ube2G2 differentially affects interactions with its partner E3 Ligases.Communications biology · 2025Article
- DET1 dynamics underlie cooperative ubiquitination by CRL4Science advances · 2025Article
- miR-379-5p affects breast cancer cell behavior by targeting UBE2E3 ubiquitin conjugating enzyme.PloS one · 2024Article
- The Role of NRF2/KEAP1 Signaling Pathway in Cancer Metabolism.International journal of molecular sciences · 2021Review
- UBE2E3 regulates cellular senescence and osteogenic differentiation of BMSCs during aging.PeerJ · 2021Article
- The Role of Conformational Dynamics in the Recognition and Regulation of Ubiquitination.Molecules (Basel, Switzerland) · 2020Review
- E2 ubiquitin-conjugating enzyme UBE2L6 promotes Senecavirus A proliferation by stabilizing the viral RNA polymerase.PLoS pathogens · 2020Article
- Structural and Functional Analysis of Ubiquitin-based Inhibitors That Target the Backsides of E2 Enzymes.Journal of molecular biology · 2020Article
- Structural basis of generic versus specific E2-RING E3 interactions in protein ubiquitination.Protein science : a publication of the Protein Society · 2019Review
- The DNA repair protein SHPRH is a nucleosome-stimulated ATPase and a nucleosome-E3 ubiquitin ligase.Epigenetics & chromatin · 2019Article
- Cbl interacts with multiple E2s in vitro and in cells.PloS one · 2019Article
- Article
- Loss of the ubiquitin conjugating enzyme UBE2E3 induces cellular senescence.Redox biology · 2018Article
- A muscle-specific MuRF1-E2 network requires stabilization of MuRF1-E2 complexes by telethonin, a newly identified substrate.Journal of cachexia, sarcopenia and muscle · 2018Article
- Role of E2-RING Interactions in Governing RNF4-Mediated Substrate Ubiquitination.Journal of molecular biology · 2016Article
- A MUB E2 structure reveals E1 selectivity between cognate ubiquitin E2s in eukaryotes.Nature communications · 2016Article
- E2 enzymes: more than just middle men.Cell research · 2016Review
- Insights into Ubiquitination from the Unique Clamp-like Binding of the RING E3 AO7 to the E2 UbcH5B.The Journal of biological chemistry · 2015Article
- Role of a non-canonical surface of Rad6 in ubiquitin conjugating activity.Nucleic acids research · 2015Article
- Role of E2-Ub-conjugating enzymes during skeletal muscle atrophy.Frontiers in physiology · 2015Review
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6 authors.
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Abstract
Proteins can be modified on lysines (K) with a single ubiquitin (Ub) or with polymers of Ub (polyUb). These different configurations and their respective topologies are primary factors for determining whether substrates are targeted to the proteasome for degradation or directed to nonproteolytic outcomes. We report here on the intrinsic ubiquitylation properties of UbcM2 (UBE2E3/UbcH9), a conserved Ub-conjugating enzyme linked to cell proliferation, development, and the cellular antioxidant defense system. Using a fully recombinant ubiquitylation assay, we show that UbcM2 is severely limited in its ability to synthesize polyUb chains with wild-type Ub. Restriction to monoubiquitylation is governed by multiple residues on the backside of the enzyme, far removed from its active site, and by lysine 48 of Ub. UbcM2 with mutated backside residues can synthesize K63-linked polyUb chains and to a lesser extent K6- and K48-linked chains. Additionally, we identified a single residue on the backside of the enzyme that promotes monoubiquitylation. Together, these findings reveal that a combination of noncatalytic residues within the Ubc catalytic core domain of UbcM2 as well as a lysine(s) within Ub can relegate a Ub-conjugating enzyme to monoubiquitylate its cognate targets despite having the latent capacity to construct polyUb chains. The two-fold mechanism for restricting activity to monoubiquitylation provides added insurance that UbcM2 will not build polyUb chains on its substrates, even under conditions of high local Ub concentrations.
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