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...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2020-01-01
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| Series: | PLoS ONE |
| Online Access: | https://doi.org/10.1371/journal.pone.0241576 |
| _version_ | 1819025635304013824 |
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| author | Nadine Camougrand Pierre Vigié Cécile Gonzalez Stéphen Manon Ingrid Bhatia-Kiššová |
| author_facet | Nadine Camougrand Pierre Vigié Cécile Gonzalez Stéphen Manon Ingrid Bhatia-Kiššová |
| author_sort | Nadine Camougrand |
| collection | DOAJ |
| 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. |
| first_indexed | 2024-12-21T05:13:49Z |
| format | Article |
| id | doaj.art-b401bd0469a74aeb9c2839e399fce089 |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-21T05:13:49Z |
| publishDate | 2020-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-b401bd0469a74aeb9c2839e399fce0892022-12-21T19:14:58ZengPublic Library of Science (PLoS)PLoS ONE1932-62032020-01-011512e024157610.1371/journal.pone.0241576The yeast mitophagy receptor Atg32 is ubiquitinated and degraded by the proteasome.Nadine CamougrandPierre VigiéCécile GonzalezStéphen ManonIngrid Bhatia-KiššováMitophagy, 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.https://doi.org/10.1371/journal.pone.0241576 |
| spellingShingle | Nadine Camougrand Pierre Vigié Cécile Gonzalez Stéphen Manon Ingrid Bhatia-Kiššová The yeast mitophagy receptor Atg32 is ubiquitinated and degraded by the proteasome. PLoS ONE |
| 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 |
| url | https://doi.org/10.1371/journal.pone.0241576 |
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