Efficiency of the four proteasome subtypes to degrade ubiquitinated or oxidized proteins
The proteasome is responsible for selective degradation of proteins. It exists in mammalian cells under four main subtypes, which differ by the combination of their catalytic subunits: the standard proteasome (β1–β2–β5), the immunoproteasome (β1i–β2i–β5i) and the two intermediate proteasomes (β1–β2–...
| Main Authors: | , , , , , , , , , , |
|---|---|
| Format: | Journal article |
| Language: | English |
| Published: |
Springer Nature
2020
|
| _version_ | 1826261205417721856 |
|---|---|
| author | Abi Habib, J De Plaen, E Stroobant, V Zivkovic, D Bousquet, M-P Guillaume, B Wahni, K Messens, J Busse, A Vigneron, N Van den Eynde, BJ |
| author_facet | Abi Habib, J De Plaen, E Stroobant, V Zivkovic, D Bousquet, M-P Guillaume, B Wahni, K Messens, J Busse, A Vigneron, N Van den Eynde, BJ |
| author_sort | Abi Habib, J |
| collection | OXFORD |
| description | The proteasome is responsible for selective degradation of proteins. It exists in mammalian cells under four main subtypes, which differ by the combination of their catalytic subunits: the standard proteasome (β1–β2–β5), the immunoproteasome (β1i–β2i–β5i) and the two intermediate proteasomes (β1–β2–β5i and β1i–β2–β5i). The efficiency of the four proteasome subtypes to degrade ubiquitinated or oxidized proteins remains unclear. Using cells expressing exclusively one proteasome subtype, we observed that ubiquitinated p21 and c-myc were degraded at similar rates, indicating that the four 26S proteasomes degrade ubiquitinated proteins equally well. Under oxidative stress, we observed a partial dissociation of 26S into 20S proteasomes, which can degrade non-ubiquitinated oxidized proteins. Oxidized calmodulin and hemoglobin were best degraded in vitro by the three β5i-containing 20S proteasomes, while their native forms were not degraded. Circular dichroism analyses indicated that ubiquitin-independent recognition of oxidized proteins by 20S proteasomes was triggered by the disruption of their structure. Accordingly, β5i-containing 20S proteasomes degraded unoxidized naturally disordered protein tau, while 26S proteasomes did not. Our results suggest that the three β5i-containing 20S proteasomes, namely the immunoproteasome and the two intermediate proteasomes, might help cells to eliminate proteins containing disordered domains, including those induced by oxidative stress. |
| first_indexed | 2024-03-06T19:17:52Z |
| format | Journal article |
| id | oxford-uuid:19099653-08e9-4671-a191-65f15c239425 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T19:17:52Z |
| publishDate | 2020 |
| publisher | Springer Nature |
| record_format | dspace |
| spelling | oxford-uuid:19099653-08e9-4671-a191-65f15c2394252022-03-26T10:46:39ZEfficiency of the four proteasome subtypes to degrade ubiquitinated or oxidized proteinsJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:19099653-08e9-4671-a191-65f15c239425EnglishSymplectic ElementsSpringer Nature2020Abi Habib, JDe Plaen, EStroobant, VZivkovic, DBousquet, M-PGuillaume, BWahni, KMessens, JBusse, AVigneron, NVan den Eynde, BJThe proteasome is responsible for selective degradation of proteins. It exists in mammalian cells under four main subtypes, which differ by the combination of their catalytic subunits: the standard proteasome (β1–β2–β5), the immunoproteasome (β1i–β2i–β5i) and the two intermediate proteasomes (β1–β2–β5i and β1i–β2–β5i). The efficiency of the four proteasome subtypes to degrade ubiquitinated or oxidized proteins remains unclear. Using cells expressing exclusively one proteasome subtype, we observed that ubiquitinated p21 and c-myc were degraded at similar rates, indicating that the four 26S proteasomes degrade ubiquitinated proteins equally well. Under oxidative stress, we observed a partial dissociation of 26S into 20S proteasomes, which can degrade non-ubiquitinated oxidized proteins. Oxidized calmodulin and hemoglobin were best degraded in vitro by the three β5i-containing 20S proteasomes, while their native forms were not degraded. Circular dichroism analyses indicated that ubiquitin-independent recognition of oxidized proteins by 20S proteasomes was triggered by the disruption of their structure. Accordingly, β5i-containing 20S proteasomes degraded unoxidized naturally disordered protein tau, while 26S proteasomes did not. Our results suggest that the three β5i-containing 20S proteasomes, namely the immunoproteasome and the two intermediate proteasomes, might help cells to eliminate proteins containing disordered domains, including those induced by oxidative stress. |
| spellingShingle | Abi Habib, J De Plaen, E Stroobant, V Zivkovic, D Bousquet, M-P Guillaume, B Wahni, K Messens, J Busse, A Vigneron, N Van den Eynde, BJ Efficiency of the four proteasome subtypes to degrade ubiquitinated or oxidized proteins |
| title | Efficiency of the four proteasome subtypes to degrade ubiquitinated or oxidized proteins |
| title_full | Efficiency of the four proteasome subtypes to degrade ubiquitinated or oxidized proteins |
| title_fullStr | Efficiency of the four proteasome subtypes to degrade ubiquitinated or oxidized proteins |
| title_full_unstemmed | Efficiency of the four proteasome subtypes to degrade ubiquitinated or oxidized proteins |
| title_short | Efficiency of the four proteasome subtypes to degrade ubiquitinated or oxidized proteins |
| title_sort | efficiency of the four proteasome subtypes to degrade ubiquitinated or oxidized proteins |
| work_keys_str_mv | AT abihabibj efficiencyofthefourproteasomesubtypestodegradeubiquitinatedoroxidizedproteins AT deplaene efficiencyofthefourproteasomesubtypestodegradeubiquitinatedoroxidizedproteins AT stroobantv efficiencyofthefourproteasomesubtypestodegradeubiquitinatedoroxidizedproteins AT zivkovicd efficiencyofthefourproteasomesubtypestodegradeubiquitinatedoroxidizedproteins AT bousquetmp efficiencyofthefourproteasomesubtypestodegradeubiquitinatedoroxidizedproteins AT guillaumeb efficiencyofthefourproteasomesubtypestodegradeubiquitinatedoroxidizedproteins AT wahnik efficiencyofthefourproteasomesubtypestodegradeubiquitinatedoroxidizedproteins AT messensj efficiencyofthefourproteasomesubtypestodegradeubiquitinatedoroxidizedproteins AT bussea efficiencyofthefourproteasomesubtypestodegradeubiquitinatedoroxidizedproteins AT vigneronn efficiencyofthefourproteasomesubtypestodegradeubiquitinatedoroxidizedproteins AT vandeneyndebj efficiencyofthefourproteasomesubtypestodegradeubiquitinatedoroxidizedproteins |