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Proximity Ligation In situ Assay is a Powerful Tool to Monitor Specific ATG Protein Interactions following Autophagy Induction

Macroautophagy is a highly regulated intracellular degradation process which has been extensively studied over the last decade. This pathway has been initially described as a non selective process inducing the degradation of parts of the cytoplasm as well as organelles at random. Nevertheless, over...

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Autores principales: Gauthier, Thierry, Claude-Taupin, Aurore, Delage-Mourroux, Régis, Boyer-Guittaut, Michaël, Hervouet, Eric
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4452782/
https://www.ncbi.nlm.nih.gov/pubmed/26034986
http://dx.doi.org/10.1371/journal.pone.0128701
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author Gauthier, Thierry
Claude-Taupin, Aurore
Delage-Mourroux, Régis
Boyer-Guittaut, Michaël
Hervouet, Eric
author_facet Gauthier, Thierry
Claude-Taupin, Aurore
Delage-Mourroux, Régis
Boyer-Guittaut, Michaël
Hervouet, Eric
author_sort Gauthier, Thierry
collection PubMed
description Macroautophagy is a highly regulated intracellular degradation process which has been extensively studied over the last decade. This pathway has been initially described as a non selective process inducing the degradation of parts of the cytoplasm as well as organelles at random. Nevertheless, over the last few years, new research highlighted the existence of a more selective autophagy pathway specifically recruiting some organelles or aggregates to the autophagosomes in order to induce their degradation. These selective autophagy pathways such as aggrephagy, mitophagy, pexophagy or xenophagy, involve the intervention of a cargo, the material to be degraded, cargo adapters, the molecules allowing the recruitment of the cargo to the autophagosome, and the proteins of the ATG8 family which link the cargo adapters to the autophagosome. One of the main questions which now remain is to develop new techniques and protocols able to discriminate between these different types of induced autophagy. In our work, we studied the possibility to use the P-LISA technique, which has been recently developed to study endogenous in vivo protein interactions, as a new technique to characterize the ATG proteins specifically involved in bulk or selective autophagy. In this manuscript, we indeed demonstrate that this technique allows the study of endogenous ATG protein interactions in cells following autophagy induction, but more interestingly that this technique might be used to characterize the ATG proteins involved in selective autophagy.
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spelling pubmed-44527822015-06-09 Proximity Ligation In situ Assay is a Powerful Tool to Monitor Specific ATG Protein Interactions following Autophagy Induction Gauthier, Thierry Claude-Taupin, Aurore Delage-Mourroux, Régis Boyer-Guittaut, Michaël Hervouet, Eric PLoS One Research Article Macroautophagy is a highly regulated intracellular degradation process which has been extensively studied over the last decade. This pathway has been initially described as a non selective process inducing the degradation of parts of the cytoplasm as well as organelles at random. Nevertheless, over the last few years, new research highlighted the existence of a more selective autophagy pathway specifically recruiting some organelles or aggregates to the autophagosomes in order to induce their degradation. These selective autophagy pathways such as aggrephagy, mitophagy, pexophagy or xenophagy, involve the intervention of a cargo, the material to be degraded, cargo adapters, the molecules allowing the recruitment of the cargo to the autophagosome, and the proteins of the ATG8 family which link the cargo adapters to the autophagosome. One of the main questions which now remain is to develop new techniques and protocols able to discriminate between these different types of induced autophagy. In our work, we studied the possibility to use the P-LISA technique, which has been recently developed to study endogenous in vivo protein interactions, as a new technique to characterize the ATG proteins specifically involved in bulk or selective autophagy. In this manuscript, we indeed demonstrate that this technique allows the study of endogenous ATG protein interactions in cells following autophagy induction, but more interestingly that this technique might be used to characterize the ATG proteins involved in selective autophagy. Public Library of Science 2015-06-02 /pmc/articles/PMC4452782/ /pubmed/26034986 http://dx.doi.org/10.1371/journal.pone.0128701 Text en © 2015 Gauthier et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Gauthier, Thierry
Claude-Taupin, Aurore
Delage-Mourroux, Régis
Boyer-Guittaut, Michaël
Hervouet, Eric
Proximity Ligation In situ Assay is a Powerful Tool to Monitor Specific ATG Protein Interactions following Autophagy Induction
title Proximity Ligation In situ Assay is a Powerful Tool to Monitor Specific ATG Protein Interactions following Autophagy Induction
title_full Proximity Ligation In situ Assay is a Powerful Tool to Monitor Specific ATG Protein Interactions following Autophagy Induction
title_fullStr Proximity Ligation In situ Assay is a Powerful Tool to Monitor Specific ATG Protein Interactions following Autophagy Induction
title_full_unstemmed Proximity Ligation In situ Assay is a Powerful Tool to Monitor Specific ATG Protein Interactions following Autophagy Induction
title_short Proximity Ligation In situ Assay is a Powerful Tool to Monitor Specific ATG Protein Interactions following Autophagy Induction
title_sort proximity ligation in situ assay is a powerful tool to monitor specific atg protein interactions following autophagy induction
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4452782/
https://www.ncbi.nlm.nih.gov/pubmed/26034986
http://dx.doi.org/10.1371/journal.pone.0128701
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