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The yeast mitophagy receptor Atg32 is ubiquitinated and degraded by the proteasome
Mitophagy, the process that degrades mitochondria selectively through autophagy, is involved in the quality control of mitochondria in cells grown under respiratory conditions. In yeast, the presence of the Atg32 protein on the outer mitochondrial membrane allows for the recognition and targeting of...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7757876/ https://www.ncbi.nlm.nih.gov/pubmed/33362225 http://dx.doi.org/10.1371/journal.pone.0241576 |
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author | Camougrand, Nadine Vigié, Pierre Gonzalez, Cécile Manon, Stéphen Bhatia-Kiššová, Ingrid |
author_facet | Camougrand, Nadine Vigié, Pierre Gonzalez, Cécile Manon, Stéphen Bhatia-Kiššová, Ingrid |
author_sort | Camougrand, Nadine |
collection | PubMed |
description | Mitophagy, the process that degrades mitochondria selectively through autophagy, is involved in the quality control of mitochondria in cells grown under respiratory conditions. In yeast, the presence of the Atg32 protein on the outer mitochondrial membrane allows for the recognition and targeting of superfluous or damaged mitochondria for degradation. Post-translational modifications such as phosphorylation are crucial for the execution of mitophagy. In our study we monitor the stability of Atg32 protein in the yeast S. cerevisiae and show that Atg32 is degraded under normal growth conditions, upon starvation or rapamycin treatment. The Atg32 turnover can be prevented by inhibition of the proteasome activity, suggesting that Atg32 is also ubiquitinated. Mass spectrometry analysis of purified Atg32 protein revealed that at least lysine residue in position 282 is ubiquitinated. Interestingly, the replacement of lysine 282 with alanine impaired Atg32 degradation only partially in the course of cell growth, suggesting that additional lysine residues on Atg32 might also be ubiquitinated. Our results provide the foundation to further elucidate the physiological significance of Atg32 turnover and the interplay between mitophagy and the proteasome. |
format | Online Article Text |
id | pubmed-7757876 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-77578762021-01-06 The yeast mitophagy receptor Atg32 is ubiquitinated and degraded by the proteasome Camougrand, Nadine Vigié, Pierre Gonzalez, Cécile Manon, Stéphen Bhatia-Kiššová, Ingrid PLoS One Research Article Mitophagy, the process that degrades mitochondria selectively through autophagy, is involved in the quality control of mitochondria in cells grown under respiratory conditions. In yeast, the presence of the Atg32 protein on the outer mitochondrial membrane allows for the recognition and targeting of superfluous or damaged mitochondria for degradation. Post-translational modifications such as phosphorylation are crucial for the execution of mitophagy. In our study we monitor the stability of Atg32 protein in the yeast S. cerevisiae and show that Atg32 is degraded under normal growth conditions, upon starvation or rapamycin treatment. The Atg32 turnover can be prevented by inhibition of the proteasome activity, suggesting that Atg32 is also ubiquitinated. Mass spectrometry analysis of purified Atg32 protein revealed that at least lysine residue in position 282 is ubiquitinated. Interestingly, the replacement of lysine 282 with alanine impaired Atg32 degradation only partially in the course of cell growth, suggesting that additional lysine residues on Atg32 might also be ubiquitinated. Our results provide the foundation to further elucidate the physiological significance of Atg32 turnover and the interplay between mitophagy and the proteasome. Public Library of Science 2020-12-23 /pmc/articles/PMC7757876/ /pubmed/33362225 http://dx.doi.org/10.1371/journal.pone.0241576 Text en © 2020 Camougrand et al http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. |
spellingShingle | Research Article Camougrand, Nadine Vigié, Pierre Gonzalez, Cécile Manon, Stéphen Bhatia-Kiššová, Ingrid The yeast mitophagy receptor Atg32 is ubiquitinated and degraded by the proteasome |
title | The yeast mitophagy receptor Atg32 is ubiquitinated and degraded by the proteasome |
title_full | The yeast mitophagy receptor Atg32 is ubiquitinated and degraded by the proteasome |
title_fullStr | The yeast mitophagy receptor Atg32 is ubiquitinated and degraded by the proteasome |
title_full_unstemmed | The yeast mitophagy receptor Atg32 is ubiquitinated and degraded by the proteasome |
title_short | The yeast mitophagy receptor Atg32 is ubiquitinated and degraded by the proteasome |
title_sort | yeast mitophagy receptor atg32 is ubiquitinated and degraded by the proteasome |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7757876/ https://www.ncbi.nlm.nih.gov/pubmed/33362225 http://dx.doi.org/10.1371/journal.pone.0241576 |
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