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Showing 1–4 of 4 results
Advanced filters: Author: Fredrik Trulsson Clear advanced filters

  • Deubiquitinases (DUBs) remove ubiquitin from its target proteins. Here, authors compare the regulatory effects of the proteasome and DUBs on the ubiquitinated proteome. They find preferential sets of substrates regulated by DUBs or by the proteasome. Moreover, they find that PARP1 is hyper-ubiquitinated in response to DUB inhibition, which increases its enzymatic activity.

    • Fredrik Trulsson
    • Vyacheslav Akimov
    • Alfred C. O. Vertegaal
    ResearchOpen Access
    Nature Communications
    Volume: 13, P: 1-17

  • Here, the authors describe BioE3, a biotin-based method to discriminate direct substrates of ubiquitin E3 ligases of interest from mere interactors using proximity proteomics. BioE3 responds to chemical treatments, and works with RING- and HECT-type E3s, as well as ubiquitin-likes (e.g., SUMO).

    • Orhi Barroso-Gomila
    • Laura Merino-Cacho
    • James D. Sutherland
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-19

  • Several proteomic approaches allow the analysis of covalent protein SUMOylation, but it remains challenging to systematically study the consequences of a substrate being modified. Here, the authors combine proximity biotinylation and protein-fragment complementation to identify SUMO-dependent protein interactors.

    • Orhi Barroso-Gomila
    • Fredrik Trulsson
    • James D. Sutherland
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-19