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Showing 1–3 of 3 results
Advanced filters: Author: Leah Randles Clear advanced filters

  • 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

  • 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

  • In the proteasome, Rpn2 provides the docking site for substrate receptor Rpn13. Here the authors present the structure of human Rpn13 Pru domain bound to its binding site in Rpn2 and provide insights into the mode of action for Rpn13-targeting molecule RA190, which has anticancer properties.

    • Xiuxiu Lu
    • Urszula Nowicka
    • Kylie J. Walters
    ResearchOpen Access
    Nature Communications
    Volume: 8, P: 1-13