ArticleMolecular and cellular biology2016
Mechanism of Lysine 48 Selectivity during Polyubiquitin Chain Formation by the Ube2R1/2 Ubiquitin-Conjugating Enzyme.
Article in Molecular and cellular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 19 citations in OpenAlex.
- Linked-domain inhibitors designed to block UBE2D induce the unfolded protein response.Cell chemical biology · 2025Article
- Mechanism of degrader-targeted protein ubiquitinability.Science advances · 2024Article
- Design of linked-domain protein inhibitors of UBE2D as tools to study cellular ubiquitination.bioRxiv : the preprint server for biology · 2024Article
- Catalysis of non-canonical protein ubiquitylation by the ARIH1 ubiquitin ligase.The Biochemical journal · 2023Article
- From seeds to trees: how E2 enzymes grow ubiquitin chains.Biochemical Society transactions · 2023Review
- A siRNA screening of UBE2 family demonstrated that UBE2R1 had a high repressive effect on HIV Tat protein.Biochemistry and biophysics reports · 2022Article
- Ubiquitin and a charged loop regulate the ubiquitin E3 ligase activity of Ark2C.Nature communications · 2022Article
- Functional conservation and divergence of the helix-turn-helix motif of E2 ubiquitin-conjugating enzymes.The EMBO journal · 2022Article
- Review
- HERC5 and the ISGylation Pathway: Critical Modulators of the Antiviral Immune Response.Viruses · 2021Review
- Linkage-specific ubiquitin chain formation depends on a lysine hydrocarbon ruler.Nature chemical biology · 2021Article
- Autophagy Induction and Accumulation of Phosphorylated Tau in the Hippocampus and Prefrontal Cortex of Adult C57BL/6 Mice Subjected to Adolescent Fluoxetine Treatment.Journal of Alzheimer's disease : JAD · 2021Article
- Structural insights into E1 recognition and the ubiquitin-conjugating activity of the E2 enzyme Cdc34.Nature communications · 2019Article
- Enzymatic Logic of Ubiquitin Chain Assembly.Frontiers in physiology · 2019Review
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Lysine selectivity is of critical importance during polyubiquitin chain formation because the identity of the lysine controls the biological outcome. Ubiquitins are covalently linked in polyubiquitin chains through one of seven lysine residues on its surface and the C terminus of adjacent protomers. Lys 48-linked polyubiquitin chains signal for protein degradation; however, the structural basis for Lys 48 selectivity remains largely unknown. The ubiquitin-conjugating enzyme Ube2R1/2 has exquisite specificity for Lys 48, and computational docking of Ube2R1/2 and ubiquitin predicts that Lys 48 is guided to the active site through a key electrostatic interaction between Arg 54 on ubiquitin and Asp 143 on Ube2R1/2. The validity of this interaction was confirmed through biochemical experiments. Since structural examples involving Arg 54 in protein-ubiquitin complexes are exceedingly rare, these results provide additional insight into how ubiquitin-protein complexes can be stabilized. We discuss how these findings relate to how other ubiquitin-conjugating enzymes direct the lysine specificity of polyubiquitin chains.
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