67393.pdf
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 i...
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InTechOpen
2021
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oapen-20.500.12657-493342021-11-23T13:57:45Z Chapter Structural Insight into Regulation of the Proteasome Ub-Receptor Rpn10 Kleifeld, Oded Levin-Kravets, Olga Prag, Gali Ben-Aroya, Shay Attali, Ilan Keren-Kaplan, Tal ubiquitin receptor, crystal structure, ubiquitylated ubiquitin receptor, regulation mechanisms, cargo shuttle bic Book Industry Communication::P Mathematics & science::PS Biology, life sciences::PSB Biochemistry::PSBC Proteins 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. 2021-06-02T10:12:24Z 2021-06-02T10:12:24Z 2019 chapter ONIX_20210602_10.5772/intechopen.85283_448 https://library.oapen.org/handle/20.500.12657/49334 eng application/pdf n/a 67393.pdf InTechOpen 10.5772/intechopen.85283 10.5772/intechopen.85283 09f6769d-48ed-467d-b150-4cf2680656a1 FP7-PEOPLE-IRG-2008 231079 open access |
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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. |
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