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Three-Axis Model for Atg Recruitment in Autophagy against Salmonella

Salmonella enterica serovar Typhimurium enter epithelial cells and take up residence there. Within epithelial cells, a portion of the bacteria are surrounded by an autophagosome-like double-membrane structure, and they are still residing within the Salmonella-containing vacuole (SCV). In this paper,...

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Detalles Bibliográficos
Autores principales: Noda, Takeshi, Kageyama, Shun, Fujita, Naonobu, Yoshimori, Tamotsu
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Hindawi Publishing Corporation 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3299270/
https://www.ncbi.nlm.nih.gov/pubmed/22505927
http://dx.doi.org/10.1155/2012/389562
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author Noda, Takeshi
Kageyama, Shun
Fujita, Naonobu
Yoshimori, Tamotsu
author_facet Noda, Takeshi
Kageyama, Shun
Fujita, Naonobu
Yoshimori, Tamotsu
author_sort Noda, Takeshi
collection PubMed
description Salmonella enterica serovar Typhimurium enter epithelial cells and take up residence there. Within epithelial cells, a portion of the bacteria are surrounded by an autophagosome-like double-membrane structure, and they are still residing within the Salmonella-containing vacuole (SCV). In this paper, we will discuss how the autophagy machinery is recruited in proximity to Salmonella. The formation of this double membrane requires Atg9L1 and FIP200; these proteins are important for autophagy-specific recruitment of the PI3-kinase complex. In the absence of Atg9L1, FIP200, and PI3-kinase activity, LC3 is still recruited to the vicinity of Salmonella. We propose a novel model in which the mechanism of LC3 recruitment is separate from the generation of the isolation membrane. There exist at least three axes in Atg recruitment: ULK1 complex, Atg9L1, and Atg16L complex.
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spelling pubmed-32992702012-04-13 Three-Axis Model for Atg Recruitment in Autophagy against Salmonella Noda, Takeshi Kageyama, Shun Fujita, Naonobu Yoshimori, Tamotsu Int J Cell Biol Review Article Salmonella enterica serovar Typhimurium enter epithelial cells and take up residence there. Within epithelial cells, a portion of the bacteria are surrounded by an autophagosome-like double-membrane structure, and they are still residing within the Salmonella-containing vacuole (SCV). In this paper, we will discuss how the autophagy machinery is recruited in proximity to Salmonella. The formation of this double membrane requires Atg9L1 and FIP200; these proteins are important for autophagy-specific recruitment of the PI3-kinase complex. In the absence of Atg9L1, FIP200, and PI3-kinase activity, LC3 is still recruited to the vicinity of Salmonella. We propose a novel model in which the mechanism of LC3 recruitment is separate from the generation of the isolation membrane. There exist at least three axes in Atg recruitment: ULK1 complex, Atg9L1, and Atg16L complex. Hindawi Publishing Corporation 2012 2012-02-28 /pmc/articles/PMC3299270/ /pubmed/22505927 http://dx.doi.org/10.1155/2012/389562 Text en Copyright © 2012 Takeshi Noda et al. https://creativecommons.org/licenses/by/3.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Review Article
Noda, Takeshi
Kageyama, Shun
Fujita, Naonobu
Yoshimori, Tamotsu
Three-Axis Model for Atg Recruitment in Autophagy against Salmonella
title Three-Axis Model for Atg Recruitment in Autophagy against Salmonella
title_full Three-Axis Model for Atg Recruitment in Autophagy against Salmonella
title_fullStr Three-Axis Model for Atg Recruitment in Autophagy against Salmonella
title_full_unstemmed Three-Axis Model for Atg Recruitment in Autophagy against Salmonella
title_short Three-Axis Model for Atg Recruitment in Autophagy against Salmonella
title_sort three-axis model for atg recruitment in autophagy against salmonella
topic Review Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3299270/
https://www.ncbi.nlm.nih.gov/pubmed/22505927
http://dx.doi.org/10.1155/2012/389562
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