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        Chapter Structural Insight into Regulation of the Proteasome Ub-Receptor Rpn10

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        Author(s)
        Kleifeld, Oded
        Levin-Kravets, Olga
        Prag, Gali
        Ben-Aroya, Shay
        Attali, Ilan
        Keren-Kaplan, Tal
        Language
        English
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        Abstract
        Ubiquitylation is a posttranslational modification that determines protein fate. The ubiquitin code is written by enzymatic cascades of E1 and E2 and E3 enzymes. Ubiquitylation can be edited or erased by deubiquitylating enzymes. Ub-receptors are proteins that read and decipher the ubiquitin codes into cellular response. They harbor a ubiquitin-binding domain and a response element. Interestingly, Ub-receptors are also regulated by ubiquitylation and deubiquitylation. However, until recently, the molecular details and the significance of this regulation remained enigmatic. Rpn10 is a Ub-receptor that shuttles ubiquitylated targets to the proteasome for degradation. Here we review recent data on Rpn10, with emphasis on its regulation by ubiquitylation.
        URI
        https://library.oapen.org/handle/20.500.12657/49334
        Keywords
        ubiquitin receptor, crystal structure, ubiquitylated ubiquitin receptor, regulation mechanisms, cargo shuttle
        DOI
        10.5772/intechopen.85283
        Publisher
        InTechOpen
        Publisher website
        https://www.intechopen.com/
        Publication date and place
        2019
        Classification
        Biochemistry
        Rights
        https://creativecommons.org/licenses/by/3.0/
        • Imported or submitted locally

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        License

        • If not noted otherwise all contents are available under Attribution 4.0 International (CC BY 4.0)

        Credits

        • logo EU
        • This project received funding from the European Union's Horizon 2020 research and innovation programme under grant agreement No 683680, 810640, 871069 and 964352.

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