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The Ubp3/Bre5 deubiquitylation complex modulates COPII vesicle formation
The appropriate delivery of secretory proteins to the correct subcellular destination is an essential cellular process. In the endoplasmic reticulum (ER), secretory proteins are captured into COPII vesicles that generally exclude ER resident proteins and misfolded proteins. We previously characteriz...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley & Sons A/S
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7711842/ https://www.ncbi.nlm.nih.gov/pubmed/32975860 http://dx.doi.org/10.1111/tra.12766 |
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author | Gomez‐Navarro, Natalia Boulanger, Jérôme Miller, Elizabeth A. |
author_facet | Gomez‐Navarro, Natalia Boulanger, Jérôme Miller, Elizabeth A. |
author_sort | Gomez‐Navarro, Natalia |
collection | PubMed |
description | The appropriate delivery of secretory proteins to the correct subcellular destination is an essential cellular process. In the endoplasmic reticulum (ER), secretory proteins are captured into COPII vesicles that generally exclude ER resident proteins and misfolded proteins. We previously characterized a collection of yeast mutants that fail to enforce this sorting stringency and improperly secrete the ER chaperone, Kar2 (Copic et al., Genetics 2009). Here, we used the emp24Δ mutant strain that secretes Kar2 to identify candidate proteins that might regulate ER export, reasoning that loss of regulatory proteins would restore sorting stringency. We find that loss of the deubiquitylation complex Ubp3/Bre5 reverses all of the known phenotypes of the emp24Δ mutant, and similarly reverses Kar2 secretion of many other ER retention mutants. Based on a combination of genetic interactions and live cell imaging, we conclude that Ubp3 and Bre5 modulate COPII coat assembly at ER exit sites. Therefore, we propose that Ubp3/Bre5 influences the rate of vesicle formation from the ER that in turn can impact ER quality control events. |
format | Online Article Text |
id | pubmed-7711842 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | John Wiley & Sons A/S |
record_format | MEDLINE/PubMed |
spelling | pubmed-77118422020-12-09 The Ubp3/Bre5 deubiquitylation complex modulates COPII vesicle formation Gomez‐Navarro, Natalia Boulanger, Jérôme Miller, Elizabeth A. Traffic Original Articles The appropriate delivery of secretory proteins to the correct subcellular destination is an essential cellular process. In the endoplasmic reticulum (ER), secretory proteins are captured into COPII vesicles that generally exclude ER resident proteins and misfolded proteins. We previously characterized a collection of yeast mutants that fail to enforce this sorting stringency and improperly secrete the ER chaperone, Kar2 (Copic et al., Genetics 2009). Here, we used the emp24Δ mutant strain that secretes Kar2 to identify candidate proteins that might regulate ER export, reasoning that loss of regulatory proteins would restore sorting stringency. We find that loss of the deubiquitylation complex Ubp3/Bre5 reverses all of the known phenotypes of the emp24Δ mutant, and similarly reverses Kar2 secretion of many other ER retention mutants. Based on a combination of genetic interactions and live cell imaging, we conclude that Ubp3 and Bre5 modulate COPII coat assembly at ER exit sites. Therefore, we propose that Ubp3/Bre5 influences the rate of vesicle formation from the ER that in turn can impact ER quality control events. John Wiley & Sons A/S 2020-10-20 2020-11 /pmc/articles/PMC7711842/ /pubmed/32975860 http://dx.doi.org/10.1111/tra.12766 Text en © 2020 The Authors. Traffic published by John Wiley & Sons Ltd. This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Original Articles Gomez‐Navarro, Natalia Boulanger, Jérôme Miller, Elizabeth A. The Ubp3/Bre5 deubiquitylation complex modulates COPII vesicle formation |
title | The Ubp3/Bre5 deubiquitylation complex modulates COPII vesicle formation |
title_full | The Ubp3/Bre5 deubiquitylation complex modulates COPII vesicle formation |
title_fullStr | The Ubp3/Bre5 deubiquitylation complex modulates COPII vesicle formation |
title_full_unstemmed | The Ubp3/Bre5 deubiquitylation complex modulates COPII vesicle formation |
title_short | The Ubp3/Bre5 deubiquitylation complex modulates COPII vesicle formation |
title_sort | ubp3/bre5 deubiquitylation complex modulates copii vesicle formation |
topic | Original Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7711842/ https://www.ncbi.nlm.nih.gov/pubmed/32975860 http://dx.doi.org/10.1111/tra.12766 |
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