{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Chou HY"],"funding":["Ministry of Science and Technology, Taiwan","Academia Sinica"],"pagination":["2750-2765"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8526009"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["17(10)"],"pubmed_abstract":["Macroautophagy/autophagy is an evolutionarily conserved intracellular pathway for the degradation of cytoplasmic materials. Under stress conditions, autophagy is upregulated and double-membrane autophagosomes are formed by the expansion of phagophores. The ATG16L1 precursor fusion contributes to development of phagophore structures and is critical for the biogenesis of autophagosomes. Here, we discovered a novel role of the protein tyrosine phosphatase PTPN9 in the regulation of homotypic ATG16L1 vesicle fusion and early autophagosome formation. Depletion of PTPN9 and its <i>Drosophila</i> homolog Ptpmeg2 impaired autophagosome formation and autophagic flux. PTPN9 colocalized with ATG16L1 and was essential for homotypic fusion of ATG16L1<sup>+</sup> vesicles during starvation-induced autop"],"journal":["Autophagy"],"pubmed_title":["PTPN9-mediated dephosphorylation of VTI1B promotes ATG16L1 precursor fusion and autophagosome formation."],"pmcid":["PMC8526009"],"funding_grant_id":["101CDA-L04","MOST108-2311-B-001-014-MY3"],"pubmed_authors":["Lee YT","Chen GC","Wen JK","Hsieh PL","Lin YJ","Peng WH","Chou HY","Lin SY","Hung CC"],"additional_accession":[]},"is_claimable":false,"name":"PTPN9-mediated dephosphorylation of VTI1B promotes ATG16L1 precursor fusion and autophagosome formation.","description":"Macroautophagy/autophagy is an evolutionarily conserved intracellular pathway for the degradation of cytoplasmic materials. Under stress conditions, autophagy is upregulated and double-membrane autophagosomes are formed by the expansion of phagophores. The ATG16L1 precursor fusion contributes to development of phagophore structures and is critical for the biogenesis of autophagosomes. Here, we discovered a novel role of the protein tyrosine phosphatase PTPN9 in the regulation of homotypic ATG16L1 vesicle fusion and early autophagosome formation. Depletion of PTPN9 and its <i>Drosophila</i> homolog Ptpmeg2 impaired autophagosome formation and autophagic flux. PTPN9 colocalized with ATG16L1 and was essential for homotypic fusion of ATG16L1<sup>+</sup> vesicles during starvation-induced autop","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Oct","modification":"2025-08-18T09:52:49.597Z","creation":"2025-04-04T22:42:58.866Z"},"accession":"S-EPMC8526009","cross_references":{"pubmed":["33112705"],"doi":["10.1080/15548627.2020.1838117"]}}