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TORC1 inactivation stimulates autophagy of nucleoporin and nuclear pore complexes
The mechanisms underlying turnover of the nuclear pore complex (NPC) and the component nucleoporins (Nups) are still poorly understood. In this study, we found that the budding yeast Saccharomyces cerevisiae triggers NPC degradation by autophagy upon the inactivation of Tor kinase complex 1. This de...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Rockefeller University Press
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7337488/ https://www.ncbi.nlm.nih.gov/pubmed/32453403 http://dx.doi.org/10.1083/jcb.201910063 |
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author | Tomioka, Yui Kotani, Tetsuya Kirisako, Hiromi Oikawa, Yu Kimura, Yayoi Hirano, Hisashi Ohsumi, Yoshinori Nakatogawa, Hitoshi |
author_facet | Tomioka, Yui Kotani, Tetsuya Kirisako, Hiromi Oikawa, Yu Kimura, Yayoi Hirano, Hisashi Ohsumi, Yoshinori Nakatogawa, Hitoshi |
author_sort | Tomioka, Yui |
collection | PubMed |
description | The mechanisms underlying turnover of the nuclear pore complex (NPC) and the component nucleoporins (Nups) are still poorly understood. In this study, we found that the budding yeast Saccharomyces cerevisiae triggers NPC degradation by autophagy upon the inactivation of Tor kinase complex 1. This degradation largely depends on the selective autophagy-specific factor Atg11 and the autophagy receptor–binding ability of Atg8, suggesting that the NPC is degraded via receptor-dependent selective autophagy. Immunoelectron microscopy revealed that NPCs embedded in nuclear envelope–derived double-membrane vesicles are sequestered within autophagosomes. At least two pathways are involved in NPC degradation: Atg39-dependent nucleophagy (selective autophagy of the nucleus) and a pathway involving an unknown receptor. In addition, we found the interaction between Nup159 and Atg8 via the Atg8-family interacting motif is important for degradation of this nucleoporin not assembled into the NPC. Thus, this study provides the first evidence for autophagic degradation of the NPC and Nups, which we term “NPC-phagy” and “nucleoporinophagy.” |
format | Online Article Text |
id | pubmed-7337488 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-73374882021-01-06 TORC1 inactivation stimulates autophagy of nucleoporin and nuclear pore complexes Tomioka, Yui Kotani, Tetsuya Kirisako, Hiromi Oikawa, Yu Kimura, Yayoi Hirano, Hisashi Ohsumi, Yoshinori Nakatogawa, Hitoshi J Cell Biol Report The mechanisms underlying turnover of the nuclear pore complex (NPC) and the component nucleoporins (Nups) are still poorly understood. In this study, we found that the budding yeast Saccharomyces cerevisiae triggers NPC degradation by autophagy upon the inactivation of Tor kinase complex 1. This degradation largely depends on the selective autophagy-specific factor Atg11 and the autophagy receptor–binding ability of Atg8, suggesting that the NPC is degraded via receptor-dependent selective autophagy. Immunoelectron microscopy revealed that NPCs embedded in nuclear envelope–derived double-membrane vesicles are sequestered within autophagosomes. At least two pathways are involved in NPC degradation: Atg39-dependent nucleophagy (selective autophagy of the nucleus) and a pathway involving an unknown receptor. In addition, we found the interaction between Nup159 and Atg8 via the Atg8-family interacting motif is important for degradation of this nucleoporin not assembled into the NPC. Thus, this study provides the first evidence for autophagic degradation of the NPC and Nups, which we term “NPC-phagy” and “nucleoporinophagy.” Rockefeller University Press 2020-05-26 /pmc/articles/PMC7337488/ /pubmed/32453403 http://dx.doi.org/10.1083/jcb.201910063 Text en © 2020 Tomioka et al. http://www.rupress.org/terms/https://creativecommons.org/licenses/by-nc-sa/4.0/This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms/). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 International license, as described at https://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Report Tomioka, Yui Kotani, Tetsuya Kirisako, Hiromi Oikawa, Yu Kimura, Yayoi Hirano, Hisashi Ohsumi, Yoshinori Nakatogawa, Hitoshi TORC1 inactivation stimulates autophagy of nucleoporin and nuclear pore complexes |
title | TORC1 inactivation stimulates autophagy of nucleoporin and nuclear pore complexes |
title_full | TORC1 inactivation stimulates autophagy of nucleoporin and nuclear pore complexes |
title_fullStr | TORC1 inactivation stimulates autophagy of nucleoporin and nuclear pore complexes |
title_full_unstemmed | TORC1 inactivation stimulates autophagy of nucleoporin and nuclear pore complexes |
title_short | TORC1 inactivation stimulates autophagy of nucleoporin and nuclear pore complexes |
title_sort | torc1 inactivation stimulates autophagy of nucleoporin and nuclear pore complexes |
topic | Report |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7337488/ https://www.ncbi.nlm.nih.gov/pubmed/32453403 http://dx.doi.org/10.1083/jcb.201910063 |
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