Starvation-Dependent Regulation of Golgi Quality Control Links the TOR Signaling and Vacuolar Protein Sorting Pathways
Upon amino acid (AA) starvation and TOR inactivation, plasma-membrane-localized permeases rapidly undergo ubiquitination and internalization via the vacuolar protein sorting/multivesicular body (VPS-MVB) pathway and are degraded in the yeast vacuole. We now show that specific Golgi proteins are also...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
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Elsevier
2015-09-01
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| Series: | Cell Reports |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2211124715008979 |
| _version_ | 1818529123861004288 |
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| author | Niv Dobzinski Silvia G. Chuartzman Rachel Kama Maya Schuldiner Jeffrey E. Gerst |
| author_facet | Niv Dobzinski Silvia G. Chuartzman Rachel Kama Maya Schuldiner Jeffrey E. Gerst |
| author_sort | Niv Dobzinski |
| collection | DOAJ |
| description | Upon amino acid (AA) starvation and TOR inactivation, plasma-membrane-localized permeases rapidly undergo ubiquitination and internalization via the vacuolar protein sorting/multivesicular body (VPS-MVB) pathway and are degraded in the yeast vacuole. We now show that specific Golgi proteins are also directed to the vacuole under these conditions as part of a Golgi quality-control (GQC) process. The degradation of GQC substrates is dependent upon ubiquitination by the defective-for-SREBP-cleavage (DSC) complex, which was identified via genetic screening and includes the Tul1 E3 ligase. Using a model GQC substrate, GFP-tagged Yif1, we show that vacuolar targeting necessitates upregulation of the VPS pathway via proteasome-mediated degradation of the initial endosomal sorting complex required for transport, ESCRT-0, but not downstream ESCRT components. Thus, early cellular responses to starvation include the targeting of specific Golgi proteins for degradation, a phenomenon reminiscent of the inactivation of BTN1, the yeast Batten disease gene ortholog. |
| first_indexed | 2024-12-11T06:59:03Z |
| format | Article |
| id | doaj.art-9d6be5fb773540f29439a57c76837be2 |
| institution | Directory Open Access Journal |
| issn | 2211-1247 |
| language | English |
| last_indexed | 2024-12-11T06:59:03Z |
| publishDate | 2015-09-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Cell Reports |
| spelling | doaj.art-9d6be5fb773540f29439a57c76837be22022-12-22T01:16:39ZengElsevierCell Reports2211-12472015-09-0112111876188610.1016/j.celrep.2015.08.026Starvation-Dependent Regulation of Golgi Quality Control Links the TOR Signaling and Vacuolar Protein Sorting PathwaysNiv Dobzinski0Silvia G. Chuartzman1Rachel Kama2Maya Schuldiner3Jeffrey E. Gerst4Department of Molecular Genetics, Weizmann Institute of Science, Rehovot 76100, IsraelDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot 76100, IsraelDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot 76100, IsraelDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot 76100, IsraelDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot 76100, IsraelUpon amino acid (AA) starvation and TOR inactivation, plasma-membrane-localized permeases rapidly undergo ubiquitination and internalization via the vacuolar protein sorting/multivesicular body (VPS-MVB) pathway and are degraded in the yeast vacuole. We now show that specific Golgi proteins are also directed to the vacuole under these conditions as part of a Golgi quality-control (GQC) process. The degradation of GQC substrates is dependent upon ubiquitination by the defective-for-SREBP-cleavage (DSC) complex, which was identified via genetic screening and includes the Tul1 E3 ligase. Using a model GQC substrate, GFP-tagged Yif1, we show that vacuolar targeting necessitates upregulation of the VPS pathway via proteasome-mediated degradation of the initial endosomal sorting complex required for transport, ESCRT-0, but not downstream ESCRT components. Thus, early cellular responses to starvation include the targeting of specific Golgi proteins for degradation, a phenomenon reminiscent of the inactivation of BTN1, the yeast Batten disease gene ortholog.http://www.sciencedirect.com/science/article/pii/S2211124715008979 |
| spellingShingle | Niv Dobzinski Silvia G. Chuartzman Rachel Kama Maya Schuldiner Jeffrey E. Gerst Starvation-Dependent Regulation of Golgi Quality Control Links the TOR Signaling and Vacuolar Protein Sorting Pathways Cell Reports |
| title | Starvation-Dependent Regulation of Golgi Quality Control Links the TOR Signaling and Vacuolar Protein Sorting Pathways |
| title_full | Starvation-Dependent Regulation of Golgi Quality Control Links the TOR Signaling and Vacuolar Protein Sorting Pathways |
| title_fullStr | Starvation-Dependent Regulation of Golgi Quality Control Links the TOR Signaling and Vacuolar Protein Sorting Pathways |
| title_full_unstemmed | Starvation-Dependent Regulation of Golgi Quality Control Links the TOR Signaling and Vacuolar Protein Sorting Pathways |
| title_short | Starvation-Dependent Regulation of Golgi Quality Control Links the TOR Signaling and Vacuolar Protein Sorting Pathways |
| title_sort | starvation dependent regulation of golgi quality control links the tor signaling and vacuolar protein sorting pathways |
| url | http://www.sciencedirect.com/science/article/pii/S2211124715008979 |
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