Sorting of a multi-subunit ubiquitin ligase complex in the endolysosome system
The yeast Dsc E3 ligase complex has long been recognized as a Golgi-specific protein ubquitination system. It shares a striking sequence similarity to the Hrd1 complex that plays critical roles in the ER-associated degradation pathway. Using biochemical purification and mass spectrometry, we identif...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
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eLife Sciences Publications Ltd
2018-01-01
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| Series: | eLife |
| Subjects: | |
| Online Access: | https://elifesciences.org/articles/33116 |
| _version_ | 1818019294144888832 |
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| author | Xi Yang Felichi Mae Arines Weichao Zhang Ming Li |
| author_facet | Xi Yang Felichi Mae Arines Weichao Zhang Ming Li |
| author_sort | Xi Yang |
| collection | DOAJ |
| description | The yeast Dsc E3 ligase complex has long been recognized as a Golgi-specific protein ubquitination system. It shares a striking sequence similarity to the Hrd1 complex that plays critical roles in the ER-associated degradation pathway. Using biochemical purification and mass spectrometry, we identified two novel Dsc subunits, which we named as Gld1 and Vld1. Surprisingly, Gld1 and Vld1 do not coexist in the same complex. Instead, they compete with each other to form two functionally independent Dsc subcomplexes. The Vld1 subcomplex takes the AP3 pathway to reach the vacuole membrane, whereas the Gld1 subcomplex travels through the VPS pathway and is cycled between Golgi and endosomes by the retromer. Thus, instead of being Golgi-specific, the Dsc complex can regulate protein levels at three distinct organelles, namely Golgi, endosome, and vacuole. Our study provides a novel model of achieving multi-tasking for transmembrane ubiquitin ligases with interchangeable trafficking adaptors. |
| first_indexed | 2024-04-14T07:49:55Z |
| format | Article |
| id | doaj.art-f487aedaef024aa896f1a83dbf3ffa3d |
| institution | Directory Open Access Journal |
| issn | 2050-084X |
| language | English |
| last_indexed | 2024-04-14T07:49:55Z |
| publishDate | 2018-01-01 |
| publisher | eLife Sciences Publications Ltd |
| record_format | Article |
| series | eLife |
| spelling | doaj.art-f487aedaef024aa896f1a83dbf3ffa3d2022-12-22T02:05:13ZengeLife Sciences Publications LtdeLife2050-084X2018-01-01710.7554/eLife.33116Sorting of a multi-subunit ubiquitin ligase complex in the endolysosome systemXi Yang0https://orcid.org/0000-0003-2741-2294Felichi Mae Arines1https://orcid.org/0000-0002-5770-3116Weichao Zhang2https://orcid.org/0000-0002-0835-890XMing Li3https://orcid.org/0000-0002-1247-2377Department of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, United StatesDepartment of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, United StatesDepartment of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, United StatesDepartment of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, United StatesThe yeast Dsc E3 ligase complex has long been recognized as a Golgi-specific protein ubquitination system. It shares a striking sequence similarity to the Hrd1 complex that plays critical roles in the ER-associated degradation pathway. Using biochemical purification and mass spectrometry, we identified two novel Dsc subunits, which we named as Gld1 and Vld1. Surprisingly, Gld1 and Vld1 do not coexist in the same complex. Instead, they compete with each other to form two functionally independent Dsc subcomplexes. The Vld1 subcomplex takes the AP3 pathway to reach the vacuole membrane, whereas the Gld1 subcomplex travels through the VPS pathway and is cycled between Golgi and endosomes by the retromer. Thus, instead of being Golgi-specific, the Dsc complex can regulate protein levels at three distinct organelles, namely Golgi, endosome, and vacuole. Our study provides a novel model of achieving multi-tasking for transmembrane ubiquitin ligases with interchangeable trafficking adaptors.https://elifesciences.org/articles/33116protein ubiquitinationlysosomegolgiendosomeDsc E3 ligase complex |
| spellingShingle | Xi Yang Felichi Mae Arines Weichao Zhang Ming Li Sorting of a multi-subunit ubiquitin ligase complex in the endolysosome system eLife protein ubiquitination lysosome golgi endosome Dsc E3 ligase complex |
| title | Sorting of a multi-subunit ubiquitin ligase complex in the endolysosome system |
| title_full | Sorting of a multi-subunit ubiquitin ligase complex in the endolysosome system |
| title_fullStr | Sorting of a multi-subunit ubiquitin ligase complex in the endolysosome system |
| title_full_unstemmed | Sorting of a multi-subunit ubiquitin ligase complex in the endolysosome system |
| title_short | Sorting of a multi-subunit ubiquitin ligase complex in the endolysosome system |
| title_sort | sorting of a multi subunit ubiquitin ligase complex in the endolysosome system |
| topic | protein ubiquitination lysosome golgi endosome Dsc E3 ligase complex |
| url | https://elifesciences.org/articles/33116 |
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