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E2 enzymes in genome stability: pulling the strings behind the scenes
Osborne, Hugh C Irving, E. Forment, J. V. Schmidt, Christine K
Osborne, Hugh C
Irving, E.
Forment, J. V.
Schmidt, Christine K
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Abstract
Ubiquitin and ubiquitin-like proteins (UBLs) function as critical post-translational modifiers in the maintenance of genome stability. Ubiquitin/UBL-conjugating enzymes (E2s) are responsible, as part of a wider enzymatic cascade, for transferring single moieties or polychains of ubiquitin/UBLs to one or multiple residues on substrate proteins. Recent advances in structural and mechanistic understanding of how ubiquitin/UBL substrate attachment is orchestrated indicate that E2s can exert control over chain topology, substrate-site specificity, and downstream physiological effects to help maintain genome stability. Drug discovery efforts have typically focussed on modulating other members of the ubiquitin/UBL cascades or the ubiquitin-proteasome system. Here, we review the current standing of E2s in genome stability and revisit their potential as pharmacological targets for developing novel anti-cancer therapies.
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Date
2021
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Collections
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Article
Citation
Osborne HC, Irving E, Forment JV, Schmidt CK. E2 Enzymes in Genome Stability: Pulling the Strings Behind the Scenes. Trends Cell Biol. 2021.