{"entity": "publication", "iuid": "5371b7f2f25741168c44e0e79c3aa420", "timestamp": "2026-08-20T20:51:08.694Z", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/5371b7f2f25741168c44e0e79c3aa420.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/5371b7f2f25741168c44e0e79c3aa420"}}, "title": "ATG12-ATG5-TECPR1: an alternative E3-like complex utilized during the cellular response to lysosomal membrane damage.", "authors": [{"family": "Corkery", "given": "Dale P", "initials": "DP"}, {"family": "Wu", "given": "Yao-Wen", "initials": "YW", "orcid": "0000-0002-2573-8736", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/b915c6698bf44f3a88a880af261eb0ad.json"}}], "type": "journal article", "published": "2024-02-00", "journal": {"title": "Autophagy", "issn": "1554-8635", "volume": "20", "issue": "2", "pages": "443-444", "issn-l": "1554-8627"}, "abstract": "ATG16L1 is an essential component of the Atg8-family protein conjugation machinery, providing membrane targeting for the ATG12-ATG5 conjugate. Recently, we identified an alternative E3-like complex that functions independently of ATG16L1. This complex utilizes the autophagosome-lysosome tethering factor TECPR1 for membrane targeting. TECPR1 is recruited to damaged lysosomal membranes via a direct interaction with sphingomyelin. At the damaged membrane, TECPR1 assembles into an E3-like complex with ATG12-ATG5 to regulate unconventional LC3 lipidation and promote efficient lysosomal repair.", "doi": "10.1080/15548627.2023.2267414", "pmid": "37872727", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC10813570"}], "notes": [], "created": "2026-08-20T09:36:54.584Z", "modified": "2026-08-20T09:36:54.627Z"}