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Starvation Induces Proteasome Autophagy with Different Pathways for Core and Regulatory Particles
The proteasome is responsible for the degradation of many cellular proteins. If and how this abundant and normally stable complex is degraded by cells is largely unknown. Here we show that in yeast, upon nitrogen starvation, proteasomes are targeted for vacuolar degradation through autophagy. Using...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Society for Biochemistry and Molecular Biology
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4751371/ https://www.ncbi.nlm.nih.gov/pubmed/26670610 http://dx.doi.org/10.1074/jbc.M115.699124 |
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author | Waite, Kenrick A. Mota-Peynado, Alina De-La Vontz, Gabrielle Roelofs, Jeroen |
author_facet | Waite, Kenrick A. Mota-Peynado, Alina De-La Vontz, Gabrielle Roelofs, Jeroen |
author_sort | Waite, Kenrick A. |
collection | PubMed |
description | The proteasome is responsible for the degradation of many cellular proteins. If and how this abundant and normally stable complex is degraded by cells is largely unknown. Here we show that in yeast, upon nitrogen starvation, proteasomes are targeted for vacuolar degradation through autophagy. Using GFP-tagged proteasome subunits, we observed that autophagy of a core particle (CP) subunit depends on the deubiquitinating enzyme Ubp3, although a regulatory particle (RP) subunit does not. Furthermore, upon blocking of autophagy, RP remained largely nuclear, although CP largely localized to the cytosol as well as granular structures within the cytosol. In all, our data reveal a regulated process for the removal of proteasomes upon nitrogen starvation. This process involves CP and RP dissociation, nuclear export, and independent vacuolar targeting of CP and RP. Thus, in addition to the well characterized transcriptional up-regulation of genes encoding proteasome subunits, cells are also capable of down-regulating cellular levels of proteasomes through proteaphagy. |
format | Online Article Text |
id | pubmed-4751371 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | American Society for Biochemistry and Molecular Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-47513712016-02-23 Starvation Induces Proteasome Autophagy with Different Pathways for Core and Regulatory Particles Waite, Kenrick A. Mota-Peynado, Alina De-La Vontz, Gabrielle Roelofs, Jeroen J Biol Chem Protein Synthesis and Degradation The proteasome is responsible for the degradation of many cellular proteins. If and how this abundant and normally stable complex is degraded by cells is largely unknown. Here we show that in yeast, upon nitrogen starvation, proteasomes are targeted for vacuolar degradation through autophagy. Using GFP-tagged proteasome subunits, we observed that autophagy of a core particle (CP) subunit depends on the deubiquitinating enzyme Ubp3, although a regulatory particle (RP) subunit does not. Furthermore, upon blocking of autophagy, RP remained largely nuclear, although CP largely localized to the cytosol as well as granular structures within the cytosol. In all, our data reveal a regulated process for the removal of proteasomes upon nitrogen starvation. This process involves CP and RP dissociation, nuclear export, and independent vacuolar targeting of CP and RP. Thus, in addition to the well characterized transcriptional up-regulation of genes encoding proteasome subunits, cells are also capable of down-regulating cellular levels of proteasomes through proteaphagy. American Society for Biochemistry and Molecular Biology 2016-02-12 2015-12-15 /pmc/articles/PMC4751371/ /pubmed/26670610 http://dx.doi.org/10.1074/jbc.M115.699124 Text en © 2016 by The American Society for Biochemistry and Molecular Biology, Inc. Author's Choice—Final version free via Creative Commons CC-BY license (http://creativecommons.org/licenses/by/4.0) . |
spellingShingle | Protein Synthesis and Degradation Waite, Kenrick A. Mota-Peynado, Alina De-La Vontz, Gabrielle Roelofs, Jeroen Starvation Induces Proteasome Autophagy with Different Pathways for Core and Regulatory Particles |
title | Starvation Induces Proteasome Autophagy with Different Pathways for Core and Regulatory Particles |
title_full | Starvation Induces Proteasome Autophagy with Different Pathways for Core and Regulatory Particles |
title_fullStr | Starvation Induces Proteasome Autophagy with Different Pathways for Core and Regulatory Particles |
title_full_unstemmed | Starvation Induces Proteasome Autophagy with Different Pathways for Core and Regulatory Particles |
title_short | Starvation Induces Proteasome Autophagy with Different Pathways for Core and Regulatory Particles |
title_sort | starvation induces proteasome autophagy with different pathways for core and regulatory particles |
topic | Protein Synthesis and Degradation |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4751371/ https://www.ncbi.nlm.nih.gov/pubmed/26670610 http://dx.doi.org/10.1074/jbc.M115.699124 |
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