<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Ye H</submitter><funding>Research Grants Council, University Grants Committee</funding><funding>National Natural Science Foundation of China</funding><pagination>e2205314119</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC9618059</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>119(43)</volume><pubmed_abstract>Autophagy is an intracellular degradation system for cytoplasmic constituents which is mediated by the formation of a double-membrane organelle termed the autophagosome and its subsequent fusion with the lysosome/vacuole. The formation of the autophagosome requires membrane from the endoplasmic reticulum (ER) and is tightly regulated by a series of autophagy-related (ATG) proteins and lipids. However, how the ER contacts autophagosomes and regulates autophagy remain elusive in plants. In this study, we identified and demonstrated the roles of &lt;i>Arabidopsis&lt;/i> oxysterol-binding protein-related protein 2A (ORP2A) in mediating ER-autophagosomal membrane contacts and autophagosome biogenesis. We showed that ORP2A localizes to both ER-plasma membrane contact sites (EPCSs) and autophagosomes, </pubmed_abstract><journal>Proceedings of the National Academy of Sciences of the United States of America</journal><pubmed_title>&lt;i>Arabidopsis&lt;/i> ORP2A mediates ER-autophagosomal membrane contact sites and regulates PI3P in plant autophagy.</pubmed_title><pmcid>PMC9618059</pmcid><funding_grant_id>91854201</funding_grant_id><funding_grant_id>C4002-20W</funding_grant_id><funding_grant_id>C4033-19E</funding_grant_id><funding_grant_id>C2009-19G</funding_grant_id><funding_grant_id>CUHK14101219</funding_grant_id><funding_grant_id>C4041-18E</funding_grant_id><funding_grant_id>C4002-21EF</funding_grant_id><funding_grant_id>C4002-17G</funding_grant_id><funding_grant_id>AoE/M-05/12</funding_grant_id><funding_grant_id>R4005-18</funding_grant_id><funding_grant_id>CUHK14100818</funding_grant_id><pubmed_authors>Huang S</pubmed_authors><pubmed_authors>Jiang L</pubmed_authors><pubmed_authors>Liang Z</pubmed_authors><pubmed_authors>Yu Q</pubmed_authors><pubmed_authors>Gao J</pubmed_authors><pubmed_authors>Lin Y</pubmed_authors><pubmed_authors>Ye H</pubmed_authors></additional><is_claimable>false</is_claimable><name>&lt;i>Arabidopsis&lt;/i> ORP2A mediates ER-autophagosomal membrane contact sites and regulates PI3P in plant autophagy.</name><description>Autophagy is an intracellular degradation system for cytoplasmic constituents which is mediated by the formation of a double-membrane organelle termed the autophagosome and its subsequent fusion with the lysosome/vacuole. The formation of the autophagosome requires membrane from the endoplasmic reticulum (ER) and is tightly regulated by a series of autophagy-related (ATG) proteins and lipids. However, how the ER contacts autophagosomes and regulates autophagy remain elusive in plants. In this study, we identified and demonstrated the roles of &lt;i>Arabidopsis&lt;/i> oxysterol-binding protein-related protein 2A (ORP2A) in mediating ER-autophagosomal membrane contacts and autophagosome biogenesis. We showed that ORP2A localizes to both ER-plasma membrane contact sites (EPCSs) and autophagosomes, </description><dates><release>2022-01-01T00:00:00Z</release><publication>2022 Oct</publication><modification>2025-04-04T20:46:03.357Z</modification><creation>2025-04-04T20:46:03.357Z</creation></dates><accession>S-EPMC9618059</accession><cross_references><pubmed>36252028</pubmed><doi>10.1073/pnas.2205314119</doi></cross_references></HashMap>