The Organization and Function of the Phagophore-ER Membrane Contact Sites

Macroautophagy is characterized by the de novo formation of double-membrane vesicles termed autophagosomes. The precursor structure of autophagosomes is a membrane cistern called phagophore, which elongates through a massive acquisition of lipids until closure. The phagophore establishes membrane-co...

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Main Authors: Prado Vargas Duarte, Fulvio Reggiori
Format: Article
Language:English
Published: SAGE Publishing 2023-07-01
Series:Contact
Online Access:https://doi.org/10.1177/25152564231183898
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author Prado Vargas Duarte
Fulvio Reggiori
author_facet Prado Vargas Duarte
Fulvio Reggiori
author_sort Prado Vargas Duarte
collection DOAJ
description Macroautophagy is characterized by the de novo formation of double-membrane vesicles termed autophagosomes. The precursor structure of autophagosomes is a membrane cistern called phagophore, which elongates through a massive acquisition of lipids until closure. The phagophore establishes membrane-contact sites (MCSs) with the endoplasmic reticulum (ER), where conserved ATG proteins belonging to the ATG9 lipid scramblase, ATG2 lipid transfer and Atg18/WIPI4 β-propeller families concentrate. Several recent in vivo and in vitro studies have uncovered the relevance of these proteins and MCSs in the lipid supply required for autophagosome formation. Although important conceptual advances have been reached, the functional interrelationship between ATG9, ATG2 and Atg18/WIPI4 proteins at the phagophore-ER MCSs and their role in the phagophore expansion are not completely understood. In this review, we describe the current knowledge about the structure, interactions, localizations, and molecular functions of these proteins, with a particular emphasis on the yeast Saccharomyces cerevisiae and mammalian systems.
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spelling doaj.art-f142a00efdb24e34a01e2f17da71f7ce2023-07-27T22:33:26ZengSAGE PublishingContact2515-25642023-07-01610.1177/25152564231183898The Organization and Function of the Phagophore-ER Membrane Contact SitesPrado Vargas Duarte0Fulvio Reggiori1 Department of Biomedicine, , Aarhus C, Denmark Aarhus Institute of Advanced Studies (AIAS), , Aarhus C, DenmarkMacroautophagy is characterized by the de novo formation of double-membrane vesicles termed autophagosomes. The precursor structure of autophagosomes is a membrane cistern called phagophore, which elongates through a massive acquisition of lipids until closure. The phagophore establishes membrane-contact sites (MCSs) with the endoplasmic reticulum (ER), where conserved ATG proteins belonging to the ATG9 lipid scramblase, ATG2 lipid transfer and Atg18/WIPI4 β-propeller families concentrate. Several recent in vivo and in vitro studies have uncovered the relevance of these proteins and MCSs in the lipid supply required for autophagosome formation. Although important conceptual advances have been reached, the functional interrelationship between ATG9, ATG2 and Atg18/WIPI4 proteins at the phagophore-ER MCSs and their role in the phagophore expansion are not completely understood. In this review, we describe the current knowledge about the structure, interactions, localizations, and molecular functions of these proteins, with a particular emphasis on the yeast Saccharomyces cerevisiae and mammalian systems.https://doi.org/10.1177/25152564231183898
spellingShingle Prado Vargas Duarte
Fulvio Reggiori
The Organization and Function of the Phagophore-ER Membrane Contact Sites
Contact
title The Organization and Function of the Phagophore-ER Membrane Contact Sites
title_full The Organization and Function of the Phagophore-ER Membrane Contact Sites
title_fullStr The Organization and Function of the Phagophore-ER Membrane Contact Sites
title_full_unstemmed The Organization and Function of the Phagophore-ER Membrane Contact Sites
title_short The Organization and Function of the Phagophore-ER Membrane Contact Sites
title_sort organization and function of the phagophore er membrane contact sites
url https://doi.org/10.1177/25152564231183898
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