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Diverse Autophagosome Membrane Sources Coalesce in Recycling Endosomes
Autophagic protein degradation is mediated by autophagosomes that fuse with lysosomes, where their contents are degraded. The membrane origins of autophagosomes may involve multiple sources. However, it is unclear if and where distinct membrane sources fuse during autophagosome biogenesis. Vesicles...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Cell Press
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3791395/ https://www.ncbi.nlm.nih.gov/pubmed/24034251 http://dx.doi.org/10.1016/j.cell.2013.08.044 |
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author | Puri, Claudia Renna, Maurizio Bento, Carla F. Moreau, Kevin Rubinsztein, David C. |
author_facet | Puri, Claudia Renna, Maurizio Bento, Carla F. Moreau, Kevin Rubinsztein, David C. |
author_sort | Puri, Claudia |
collection | PubMed |
description | Autophagic protein degradation is mediated by autophagosomes that fuse with lysosomes, where their contents are degraded. The membrane origins of autophagosomes may involve multiple sources. However, it is unclear if and where distinct membrane sources fuse during autophagosome biogenesis. Vesicles containing mATG9, the only transmembrane autophagy protein, are seen in many sites, and fusions with other autophagic compartments have not been visualized in mammalian cells. We observed that mATG9 traffics from the plasma membrane to recycling endosomes in carriers that appear to be routed differently from ATG16L1-containing vesicles, another source of autophagosome membrane. mATG9- and ATG16L1-containing vesicles traffic to recycling endosomes, where VAMP3-dependent heterotypic fusions occur. These fusions correlate with autophagosome formation, and both processes are enhanced by perturbing membrane egress from recycling endosomes. Starvation, a primordial autophagy activator, reduces membrane recycling from recycling endosomes and enhances mATG9-ATG16L1 vesicle fusion. Thus, this mechanism may fine-tune physiological autophagic responses. |
format | Online Article Text |
id | pubmed-3791395 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | Cell Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-37913952013-10-07 Diverse Autophagosome Membrane Sources Coalesce in Recycling Endosomes Puri, Claudia Renna, Maurizio Bento, Carla F. Moreau, Kevin Rubinsztein, David C. Cell Article Autophagic protein degradation is mediated by autophagosomes that fuse with lysosomes, where their contents are degraded. The membrane origins of autophagosomes may involve multiple sources. However, it is unclear if and where distinct membrane sources fuse during autophagosome biogenesis. Vesicles containing mATG9, the only transmembrane autophagy protein, are seen in many sites, and fusions with other autophagic compartments have not been visualized in mammalian cells. We observed that mATG9 traffics from the plasma membrane to recycling endosomes in carriers that appear to be routed differently from ATG16L1-containing vesicles, another source of autophagosome membrane. mATG9- and ATG16L1-containing vesicles traffic to recycling endosomes, where VAMP3-dependent heterotypic fusions occur. These fusions correlate with autophagosome formation, and both processes are enhanced by perturbing membrane egress from recycling endosomes. Starvation, a primordial autophagy activator, reduces membrane recycling from recycling endosomes and enhances mATG9-ATG16L1 vesicle fusion. Thus, this mechanism may fine-tune physiological autophagic responses. Cell Press 2013-09-12 /pmc/articles/PMC3791395/ /pubmed/24034251 http://dx.doi.org/10.1016/j.cell.2013.08.044 Text en © 2013 ELL & Excerpta Medica. https://creativecommons.org/licenses/by/4.0/This work is licensed under a Creative Commons Attribution 4.0 International License (https://creativecommons.org/licenses/by/4.0/) , which allows reusers to distribute, remix, adapt, and build upon the material in any medium or format, so long as attribution is given to the creator. The license allows for commercial use. |
spellingShingle | Article Puri, Claudia Renna, Maurizio Bento, Carla F. Moreau, Kevin Rubinsztein, David C. Diverse Autophagosome Membrane Sources Coalesce in Recycling Endosomes |
title | Diverse Autophagosome Membrane Sources Coalesce in Recycling Endosomes |
title_full | Diverse Autophagosome Membrane Sources Coalesce in Recycling Endosomes |
title_fullStr | Diverse Autophagosome Membrane Sources Coalesce in Recycling Endosomes |
title_full_unstemmed | Diverse Autophagosome Membrane Sources Coalesce in Recycling Endosomes |
title_short | Diverse Autophagosome Membrane Sources Coalesce in Recycling Endosomes |
title_sort | diverse autophagosome membrane sources coalesce in recycling endosomes |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3791395/ https://www.ncbi.nlm.nih.gov/pubmed/24034251 http://dx.doi.org/10.1016/j.cell.2013.08.044 |
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