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    E2 enzymes in genome stability: pulling the strings behind the scenes

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    Authors
    Osborne, Hugh C
    Irving, E.
    Forment, J. V.
    Schmidt, Christine K
    Affiliation
    Manchester Cancer Research Centre, Division of Cancer Sciences, School of Medical Sciences, Faculty of Biology, Medicine, and Health, University of Manchester, 555 Wilmslow Road, Manchester M20 4GJ
    Issue Date
    2021
    
    Metadata
    Show full item record
    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.
    Citation
    Osborne HC, Irving E, Forment JV, Schmidt CK. E2 Enzymes in Genome Stability: Pulling the Strings Behind the Scenes. Trends Cell Biol. 2021.
    Journal
    Trends in Cell Biology
    URI
    http://hdl.handle.net/10541/623947
    DOI
    10.1016/j.tcb.2021.01.009
    PubMed ID
    33685796
    Additional Links
    https://dx.doi.org/10.1016/j.tcb.2021.01.009
    Type
    Article
    Language
    en
    ae974a485f413a2113503eed53cd6c53
    10.1016/j.tcb.2021.01.009
    Scopus Count
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    All Paterson Institute for Cancer Research

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