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Autophagosomes are formed at a distinct cellular structure
Autophagy is characterized by the formation of double-membrane vesicles called autophagosomes, which deliver bulk cytoplasmic material to the lytic compartment of the cell for degradation. Autophagosome formation is initiated by assembly and recruitment of the core autophagy machinery to distinct ce...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7588827/ https://www.ncbi.nlm.nih.gov/pubmed/32203894 http://dx.doi.org/10.1016/j.ceb.2020.02.012 |
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author | Hollenstein, David M. Kraft, Claudine |
author_facet | Hollenstein, David M. Kraft, Claudine |
author_sort | Hollenstein, David M. |
collection | PubMed |
description | Autophagy is characterized by the formation of double-membrane vesicles called autophagosomes, which deliver bulk cytoplasmic material to the lytic compartment of the cell for degradation. Autophagosome formation is initiated by assembly and recruitment of the core autophagy machinery to distinct cellular sites, referred to as phagophore assembly sites (PAS) in yeast or autophagosome formation sites in other organisms. A large number of autophagy proteins involved in the formation of autophagosomes has been identified; however, how the individual components of the PAS are assembled and how they function to generate autophagosomes remains a fundamental question. Here, we highlight recent studies that provide molecular insights into PAS organization and the role of the endoplasmic reticulum and the vacuole in autophagosome formation. |
format | Online Article Text |
id | pubmed-7588827 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Elsevier |
record_format | MEDLINE/PubMed |
spelling | pubmed-75888272020-10-30 Autophagosomes are formed at a distinct cellular structure Hollenstein, David M. Kraft, Claudine Curr Opin Cell Biol Article Autophagy is characterized by the formation of double-membrane vesicles called autophagosomes, which deliver bulk cytoplasmic material to the lytic compartment of the cell for degradation. Autophagosome formation is initiated by assembly and recruitment of the core autophagy machinery to distinct cellular sites, referred to as phagophore assembly sites (PAS) in yeast or autophagosome formation sites in other organisms. A large number of autophagy proteins involved in the formation of autophagosomes has been identified; however, how the individual components of the PAS are assembled and how they function to generate autophagosomes remains a fundamental question. Here, we highlight recent studies that provide molecular insights into PAS organization and the role of the endoplasmic reticulum and the vacuole in autophagosome formation. Elsevier 2020-08 /pmc/articles/PMC7588827/ /pubmed/32203894 http://dx.doi.org/10.1016/j.ceb.2020.02.012 Text en © 2020 The Authors http://creativecommons.org/licenses/by-nc-nd/4.0/ This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/). |
spellingShingle | Article Hollenstein, David M. Kraft, Claudine Autophagosomes are formed at a distinct cellular structure |
title | Autophagosomes are formed at a distinct cellular structure |
title_full | Autophagosomes are formed at a distinct cellular structure |
title_fullStr | Autophagosomes are formed at a distinct cellular structure |
title_full_unstemmed | Autophagosomes are formed at a distinct cellular structure |
title_short | Autophagosomes are formed at a distinct cellular structure |
title_sort | autophagosomes are formed at a distinct cellular structure |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7588827/ https://www.ncbi.nlm.nih.gov/pubmed/32203894 http://dx.doi.org/10.1016/j.ceb.2020.02.012 |
work_keys_str_mv | AT hollensteindavidm autophagosomesareformedatadistinctcellularstructure AT kraftclaudine autophagosomesareformedatadistinctcellularstructure |