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Showing 1–6 of 6 results
Advanced filters: Author: Michael J Matunis Clear advanced filters

  • A candidate-based genetic screen in Drosophila expressing 30 G4C2-repeat-containing RNAs finds that RanGAP, a key regulator of nucleocytoplasmic transport, is a potent suppressor of neurodegeneration; the defects caused by the G4C2 repeat expansions can be rescued with antisense oligonucleotides or small molecules targeting the G-quadruplexes.

    • Ke Zhang
    • Christopher J. Donnelly
    • Jeffrey D. Rothstein
    Research
    Nature
    Volume: 525, P: 56-61

  • Mediator of DNA-damage checkpoint 1 (MDC1) has a central role in repair of DNA double-strand breaks (DSBs) by both homologous recombination and nonhomologous end joining, and its function is regulated by post-translational phosphorylation, ubiquitylation and SUMOylation. In this issue, a new study by Watanabe et al. reveals that methylation of MDC1 is also critical for its function in DSB repair and specifically affects repair through BRCA1-dependent homologous recombination.

    • Jian Lu
    • Michael J Matunis
    News & Views
    Nature Structural & Molecular Biology
    Volume: 20, P: 1346-1348

  • The deubiquitinating enzyme OTUB1 binds charged E2 intermediates and prevents ubiquitin transfer. OTUB1 can also bind uncharged E2, and this interaction is now shown to stimulate OTUB1's deubiquitination activity. Thus, OTUB1–E2 complexes might regulate levels of ubiquitin conjugation in response to available free ubiquitin and the ratio of charged to uncharged E2.

    • Reuven Wiener
    • Anthony T DiBello
    • Cynthia Wolberger
    Research
    Nature Structural & Molecular Biology
    Volume: 20, P: 1033-1039

  • The activation and targeted localization of ubiquitin E2 conjugating enzymes could provide a point for regulating ubiquitin-dependent cell functions. Supporting this view, the ubiquitin charging and activation of a class of E2 enzymes has been directly linked to their nuclear import.

    • Xiang-Dong Zhang
    • Michael J Matunis
    News & Views
    Nature Cell Biology
    Volume: 7, P: 12-14

  • The crystal structure of a four-protein complex comprising a SUMO ligase (E3), a SUMOylated protein substrate, and the cognate SUMO-conjugating enzyme sheds new light on catalysis, specificity and SUMO-protein interactions.

    • Michael J Matunis
    • Cecile M Pickart
    News & Views
    Nature Structural & Molecular Biology
    Volume: 12, P: 565-566