Chapter Structural Insight into Regulation of the Proteasome Ub-Receptor Rpn10
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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2021
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| Online toegang: | ONIX_20210602_10.5772/intechopen.85283_448 |
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| author | Kleifeld, Oded Levin-Kravets, Olga Prag, Gali Ben-Aroya, Shay Attali, Ilan Keren-Kaplan, Tal |
| author_browse | Attali, Ilan Ben-Aroya, Shay Keren-Kaplan, Tal Kleifeld, Oded Levin-Kravets, Olga Prag, Gali |
| author_facet | Kleifeld, Oded Levin-Kravets, Olga Prag, Gali Ben-Aroya, Shay Attali, Ilan Keren-Kaplan, Tal |
| author_sort | Kleifeld, Oded |
| collection | Directory of Open Access Books |
| description | 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. |
| format | Online |
| id | doab-20.500.12854ir-70352 |
| institution | Directory of Open Access Books |
| language | eng |
| publishDate | 2021 |
| publishDateRange | 2021 |
| publishDateSort | 2021 |
| publisher | InTechOpen |
| publisherStr | InTechOpen |
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| spelling | doab-20.500.12854ir-703522025-08-13T14:11:55Z 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 thema EDItEUR::P Mathematics and Science::PS Biology, life sciences::PSB Biochemistry thema EDItEUR::P Mathematics and Science::PS Biology, life sciences::PSB Biochemistry 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 2019 chapter ONIX_20210602_10.5772/intechopen.85283_448 https://library.oapen.org/handle/20.500.12657/49334 https://directory.doabooks.org/handle/20.500.12854/70352 eng open access image/jpeg image/jpeg image/jpeg n/a n/a n/a https://library.oapen.org/bitstream/20.500.12657/49334/1/67393.pdf https://library.oapen.org/bitstream/20.500.12657/49334/1/67393.pdf https://library.oapen.org/bitstream/20.500.12657/49334/1/67393.pdf InTechOpen 10.5772/intechopen.85283 10.5772/intechopen.85283 035ecc65-6737-43cf-a13a-6bdf67ce01f4 open access |
| spellingShingle | ubiquitin receptor, crystal structure, ubiquitylated ubiquitin receptor, regulation mechanisms, cargo shuttle thema EDItEUR::P Mathematics and Science::PS Biology, life sciences::PSB Biochemistry thema EDItEUR::P Mathematics and Science::PS Biology, life sciences::PSB Biochemistry Kleifeld, Oded Levin-Kravets, Olga Prag, Gali Ben-Aroya, Shay Attali, Ilan Keren-Kaplan, Tal Chapter Structural Insight into Regulation of the Proteasome Ub-Receptor Rpn10 |
| title | Chapter Structural Insight into Regulation of the Proteasome Ub-Receptor Rpn10 |
| title_full | Chapter Structural Insight into Regulation of the Proteasome Ub-Receptor Rpn10 |
| title_fullStr | Chapter Structural Insight into Regulation of the Proteasome Ub-Receptor Rpn10 |
| title_full_unstemmed | Chapter Structural Insight into Regulation of the Proteasome Ub-Receptor Rpn10 |
| title_short | Chapter Structural Insight into Regulation of the Proteasome Ub-Receptor Rpn10 |
| title_sort | chapter structural insight into regulation of the proteasome ub receptor rpn10 |
| topic | ubiquitin receptor, crystal structure, ubiquitylated ubiquitin receptor, regulation mechanisms, cargo shuttle thema EDItEUR::P Mathematics and Science::PS Biology, life sciences::PSB Biochemistry thema EDItEUR::P Mathematics and Science::PS Biology, life sciences::PSB Biochemistry |
| topic_facet | ubiquitin receptor, crystal structure, ubiquitylated ubiquitin receptor, regulation mechanisms, cargo shuttle thema EDItEUR::P Mathematics and Science::PS Biology, life sciences::PSB Biochemistry thema EDItEUR::P Mathematics and Science::PS Biology, life sciences::PSB Biochemistry |
| url | ONIX_20210602_10.5772/intechopen.85283_448 |
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