{"entity": "researcher", "timestamp": "2026-08-19T21:24:29.428Z", "family": "Stjepanovic", "given": "Goran", "initials": "G", "orcid": "0000-0002-4841-9949", "affiliations": ["Kobilka Institute of Innovative Drug Discovery, School of Medicine, The Chinese University of Hong Kong, Shenzhen, Shenzhen, China. goranstjepanovic@cuhk.edu.cn."], "links": {"self": {"href": "https://publications.scilifelab.se/researcher/a25e20f893d94f8d963403da7eb2a5e1.json"}, "display": {"href": "https://publications.scilifelab.se/researcher/a25e20f893d94f8d963403da7eb2a5e1"}}, "publications": [{"entity": "publication", "iuid": "fb964a37469d46c3b8bea7ec226da10b", "links": {"self": {"href": "https://publications.scilifelab.se/publication/fb964a37469d46c3b8bea7ec226da10b.json"}, "display": {"href": "https://publications.scilifelab.se/publication/fb964a37469d46c3b8bea7ec226da10b"}}, "title": "Structural basis for lipid transfer by the ATG2A-ATG9A complex.", "authors": [{"family": "Wang", "given": "Yang", "initials": "Y", "orcid": "0000-0002-3839-0003", "researcher": {"href": "https://publications.scilifelab.se/researcher/9892fd666eaf4519bae74ec10977512e.json"}}, {"family": "Dahmane", "given": "Selma", "initials": "S"}, {"family": "Ti", "given": "Rujuan", "initials": "R", "orcid": "0000-0002-5169-8491", "researcher": {"href": "https://publications.scilifelab.se/researcher/b530a2ed7e1246b1842cfa8611ffc75d.json"}}, {"family": "Mai", "given": "Xinyi", "initials": "X", "orcid": "0009-0004-7828-061X", "researcher": {"href": "https://publications.scilifelab.se/researcher/aa46a9e3371a409c804847b14923f4a6.json"}}, {"family": "Zhu", "given": "Lizhe", "initials": "L", "orcid": "0000-0001-8252-7807", "researcher": {"href": "https://publications.scilifelab.se/researcher/8275c054d43b45b79f49c1a95b10a806.json"}}, {"family": "Carlson", "given": "Lars-Anders", "initials": "LA", "orcid": "0000-0003-2342-6488", "researcher": {"href": "https://publications.scilifelab.se/researcher/ba0e366ce21e49b48212bbed5a0a7bd1.json"}}, {"family": "Stjepanovic", "given": "Goran", "initials": "G", "orcid": "0000-0002-4841-9949", "researcher": {"href": "https://publications.scilifelab.se/researcher/a25e20f893d94f8d963403da7eb2a5e1.json"}}], "type": "journal article", "published": "2025-01-00", "journal": {"title": "Nat. Struct. Mol. Biol.", "issn": "1545-9985", "volume": "32", "issue": "1", "pages": "35-47", "issn-l": "1545-9985"}, "abstract": "Autophagy is characterized by the formation of double-membrane vesicles called autophagosomes. Autophagy-related proteins (ATGs) 2A and 9A have an essential role in autophagy by mediating lipid transfer and re-equilibration between membranes for autophagosome formation. Here we report the cryo-electron microscopy structures of human ATG2A in complex with WD-repeat protein interacting with phosphoinositides 4 (WIPI4) at 3.2 \u00c5 and the ATG2A-WIPI4-ATG9A complex at 7 \u00c5 global resolution. On the basis of molecular dynamics simulations, we propose a mechanism of lipid extraction from the donor membranes. Our analysis revealed 3:1 stoichiometry of the ATG9A-ATG2A complex, directly aligning the ATG9A lateral pore with ATG2A lipid transfer cavity, and an interaction of the ATG9A trimer with both the N-terminal and the C-terminal tip of rod-shaped ATG2A. Cryo-electron tomography of ATG2A liposome-binding states showed that ATG2A tethers lipid vesicles at different orientations. In summary, this study provides a molecular basis for the growth of the phagophore membrane and lends structural insights into spatially coupled lipid transport and re-equilibration during autophagosome formation.", "doi": "10.1038/s41594-024-01376-6", "pmid": "39174844", "labels": {"Cryo-EM": "Service"}, "xrefs": [{"db": "pii", "key": "10.1038/s41594-024-01376-6"}], "notes": [], "created": "2024-11-27T11:37:36.821Z", "modified": "2025-10-29T14:46:12.392Z"}]}