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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
            Show full item record
            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://doab-dev.siscern.org/handle/20.500.12854/165054
            Keywords
            ubiquitin receptor, crystal structure, ubiquitylated ubiquitin receptor, regulation mechanisms, cargo shuttle; thema EDItEUR::P Mathematics and Science::PS Biology, life sciences::PSB Biochemistry
            DOI
            10.5772/intechopen.85283
            Publisher
            InTechOpen
            Publication date and place
            2019
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              This project received funding from the European Union’s Horizon 2020 research and innovation programme under grant agreement No 871069.

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