<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Chumpen Ramirez S</submitter><funding>Novo Nordisk Foundation</funding><funding>Deutsche Forschungsgemeinschaft</funding><funding>Open Competition ENW-KLEIN</funding><funding>ZonMW Top</funding><funding>Horizon 2020</funding><funding>ZonMw</funding><funding>Novo Nordisk Fonden</funding><pagination>1459-1478</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC10241002</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>19(5)</volume><pubmed_abstract>During macroautophagy/autophagy, precursor cisterna known as phagophores expand and sequester portions of the cytoplasm and/or organelles, and subsequently close resulting in double-membrane transport vesicles called autophagosomes. Autophagosomes fuse with lysosomes/vacuoles to allow the degradation and recycling of their cargoes. We previously showed that sequential binding of yeast Atg2 and Atg18 to Atg9, the only conserved transmembrane protein in autophagy, at the extremities of the phagophore mediates the establishment of membrane contact sites between the phagophore and the endoplasmic reticulum. As the Atg2-Atg18 complex transfers lipids between adjacent membranes &lt;i>in vitro&lt;/i>, it has been postulated that this activity and the scramblase activity of the trimers formed by Atg9 ar</pubmed_abstract><journal>Autophagy</journal><pubmed_title>--Atg9 interactions via its transmembrane domains are required for phagophore expansion during autophagy.</pubmed_title><pmcid>PMC10241002</pmcid><funding_grant_id>91217002</funding_grant_id><funding_grant_id>OCENW.KLEIN.118]; [SFB 944</funding_grant_id><funding_grant_id>0066384</funding_grant_id><funding_grant_id>NNF21OC0066384</funding_grant_id><funding_grant_id>P26].</funding_grant_id><funding_grant_id>Marie Skłodowska Curie ETN (765912)</funding_grant_id><funding_grant_id>UN111/13-1</funding_grant_id><pubmed_authors>Margheritis E</pubmed_authors><pubmed_authors>Cosentino K</pubmed_authors><pubmed_authors>Reggiori F</pubmed_authors><pubmed_authors>Chumpen Ramirez S</pubmed_authors><pubmed_authors>Gomez-Sanchez R</pubmed_authors><pubmed_authors>Ungermann C</pubmed_authors><pubmed_authors>Verlhac P</pubmed_authors><pubmed_authors>Hardenberg R</pubmed_authors></additional><is_claimable>false</is_claimable><name>--Atg9 interactions via its transmembrane domains are required for phagophore expansion during autophagy.</name><description>During macroautophagy/autophagy, precursor cisterna known as phagophores expand and sequester portions of the cytoplasm and/or organelles, and subsequently close resulting in double-membrane transport vesicles called autophagosomes. Autophagosomes fuse with lysosomes/vacuoles to allow the degradation and recycling of their cargoes. We previously showed that sequential binding of yeast Atg2 and Atg18 to Atg9, the only conserved transmembrane protein in autophagy, at the extremities of the phagophore mediates the establishment of membrane contact sites between the phagophore and the endoplasmic reticulum. As the Atg2-Atg18 complex transfers lipids between adjacent membranes &lt;i>in vitro&lt;/i>, it has been postulated that this activity and the scramblase activity of the trimers formed by Atg9 ar</description><dates><release>2023-01-01T00:00:00Z</release><publication>2023 May</publication><modification>2026-05-05T02:54:15.649Z</modification><creation>2025-04-04T14:39:42.653Z</creation></dates><accession>S-EPMC10241002</accession><cross_references><pubmed>36354155</pubmed><doi>10.1080/15548627.2022.2136340</doi></cross_references></HashMap>