{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"submitter":["De Tito S"],"funding":["Cancer Research UK","European Research Council","Medical Research Council","Dutch Research Council (NWO)","Wellcome Trust","Biotechnology and Biological Sciences Research Council"],"pubmed_abstract":["Lysosome damage activates multiple pathways to prevent lysosome-dependent cell death, including a repair mechanism involving endoplasmic reticulum (ER)-lysosome membrane contact sites, phosphatidylinositol 4-kinase-2a (PI4K2A), phosphatidylinositol-4 phosphate (PI4P), and oxysterol-binding protein-like proteins (OSBPLs) lipid transfer proteins. PI4K2A localizes to the trans-Golgi network and endosomes, yet how it is delivered to damaged lysosomes remains unknown. During acute sterile damage and damage caused by intracellular bacteria, we show that ATG9A-containing vesicles perform a critical role in delivering PI4K2A to damaged lysosomes. ADP ribosylation factor interacting protein 2 (ARFIP2), a component of ATG9A vesicles, binds and sequesters PI4P on lysosomes, balancing OSBPL-dependent "],"journal":["Developmental cell"],"pagination":["S1534-5807(25)00318-1"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7617826"],"repository":["biostudies-literature"],"pubmed_title":["ATG9A and ARFIP2 cooperate to control PI4P levels for lysosomal repair."],"pmcid":["PMC7617826"],"funding_grant_id":["BB/R011834/1","788708","CC2081","CC2134","184.034.014"],"pubmed_authors":["de Heus C","Pellegrino E","De Tito S","Almacellas E","Hervas JH","Klumperman J","Tooze SA","Zhang W","Dai Yu D","Gutierrez M","Millard E","Thurston TLM","Panagi I","Fogde D","Queval C"],"additional_accession":[]},"is_claimable":false,"name":"ATG9A and ARFIP2 cooperate to control PI4P levels for lysosomal repair.","description":"Lysosome damage activates multiple pathways to prevent lysosome-dependent cell death, including a repair mechanism involving endoplasmic reticulum (ER)-lysosome membrane contact sites, phosphatidylinositol 4-kinase-2a (PI4K2A), phosphatidylinositol-4 phosphate (PI4P), and oxysterol-binding protein-like proteins (OSBPLs) lipid transfer proteins. PI4K2A localizes to the trans-Golgi network and endosomes, yet how it is delivered to damaged lysosomes remains unknown. During acute sterile damage and damage caused by intracellular bacteria, we show that ATG9A-containing vesicles perform a critical role in delivering PI4K2A to damaged lysosomes. ADP ribosylation factor interacting protein 2 (ARFIP2), a component of ATG9A vesicles, binds and sequesters PI4P on lysosomes, balancing OSBPL-dependent ","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 May","modification":"2026-06-02T08:44:41.426Z","creation":"2026-04-16T03:12:48.362Z"},"accession":"S-EPMC7617826","cross_references":{"pubmed":["40460835"],"doi":["10.1016/j.devcel.2025.05.007"]}}