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Showing 1–10 of 10 results
Advanced filters: Author: Suzanne Elsasser Clear advanced filters

  • The interplay of the proteasome and deubiquitinase Ubp6 is crucial for the degradation of ubiquitylated substrates. Here, the authors provide structural insights into the allosteric mechanism by which the activities of both Ubp6 and the proteasome are regulated.

    • Ka Ying Sharon Hung
    • Sven Klumpe
    • Daniel Finley
    ResearchOpen Access
    Nature Communications
    Volume: 13, P: 1-13

  • The 26S proteasome is a multisubunit complex that selectively degrades ubiquitin conjugated proteins. Two studies (this Article and the Letter Dikic doi:10.1038/nature06924) show that a known component of the proteasome, Rpn13, functions as a novel ubiquitin binding receptor, and structural studies reveal a novel mode of ubiquitin recognition. Rpn13 is also a receptor for a deubiquitinating enzyme, suggesting a linkage between ubiquitin chain recognition and disassembly.

    • Koraljka Husnjak
    • Suzanne Elsasser
    • Ivan Dikic
    Research
    Nature
    Volume: 453, P: 481-488

  • The 26S proteasome is a multisubunit complex that selectively degrades ubiquitin conjugated proteins. Two studies (this Letter and the Article Dikic doi:10.1038/nature06926) show that a known component of the proteasome, Rpn13, functions as a novel ubiquitin binding receptor, and structural studies reveal a novel mode of ubiquitin recognition. Rpn13 is also a receptor for a deubiquitinating enzyme, suggesting a linkage between ubiquitin chain recognition and disassembly.

    • Patrick Schreiner
    • Xiang Chen
    • Michael Groll
    Research
    Nature
    Volume: 453, P: 548-552

  • Ubiquitylated proteins are degraded by the proteasome and the three proteasome subunits Rpn10, Rpn13 and Rpn1 recognize ubiquitin chains. Here the authors employ biochemical and kinetic assays and characterise the ubiquitin chain type specificities of these three ubiquitin receptors.

    • Kirby Martinez-Fonts
    • Caroline Davis
    • Andreas Matouschek
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-16

  • In the ubiquitin–proteasome system, substrates destined for destruction are modified with ubiquitin chains and then degraded by the proteasome. These authors reveal a regulatory mechanism in which proteasomal activity is modulated by the length of ubiquitin chains in human cells. They find that deubiquitinating enzyme USP14 can inhibit the degradation of ubiquitin-conjugated substrates by trimming ubiquitin chains, and that stimulation of proteasome activity may be used to reduce the levels of toxic proteins in cells.

    • Byung-Hoon Lee
    • Min Jae Lee
    • Daniel Finley
    Research
    Nature
    Volume: 467, P: 179-184

  • Rad23 accompanies ubiquitinated substrates to the proteasome for destruction but manages to avoid degradation. In this study, Fishbainet al.show that Rad23 escapes because it lacks an effective initiation region; therefore, the proteasome is unable to engage the protein and unfold it.

    • Susan Fishbain
    • Sumit Prakash
    • Andreas Matouschek
    Research
    Nature Communications
    Volume: 2, P: 1-9

  • The proteasome-associated enzyme USP14 regulates protein degradation by removing ubiquitin from proteins; here it is shown that USP14 removes ubiquitin chains from in vitro generated cyclin B conjugates en bloc and within milliseconds, before the proteasome has a chance to initiate degradation, and proceeds until a single chain remains.

    • Byung-Hoon Lee
    • Ying Lu
    • Daniel Finley
    Research
    Nature
    Volume: 532, P: 398-401