Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Structural basis for lipid transfer by the ATG2A-ATG9A complex.
Journal, issue, pages	Nat Struct Mol Biol, Vol. 32, Issue 1, Page 35-47, Year 2025
Publish date	Aug 22, 2024
Authors	Yang Wang / Selma Dahmane / Rujuan Ti / Xinyi Mai / Lizhe Zhu / Lars-Anders Carlson / Goran Stjepanovic /
PubMed 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 ...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 Å and the ATG2A-WIPI4-ATG9A complex at 7 Å 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.
External links	Nat Struct Mol Biol / PubMed:39174844
Methods	EM (single particle) / EM (tomography)
Resolution	3.23 - 7.05 Å
Structure data	37086 8kbx EMDB-37086, PDB-8kbx: Cryo-EM structure of human ATG2A-WIPI4 complex Method: EM (single particle) / Resolution: 3.23 Å 37087 8kby EMDB-37087: Cryo-EM structure of ATG2A-WIPI4 complex PDB-8kby: Cryo-EM structure of ATG2A Method: EM (single particle) / Resolution: 3.23 Å 37088 8kbz EMDB-37088, PDB-8kbz: Cryo-EM structure of human ATG9A in LMNG micelles Method: EM (single particle) / Resolution: 3.97 Å 37091 8kc3 EMDB-37091, PDB-8kc3: Cryo-EM structure of human C-terminally bound ATG9A-ATG2A-WIPI4 complex Method: EM (single particle) / Resolution: 7.0 Å 38839 8y1l EMDB-38839, PDB-8y1l: Cryo-EM structure of human N-terminally bound ATG9A-ATG2A-WIPI4 complex Method: EM (single particle) / Resolution: 7.05 Å EMDB-50658: Cryo-electron tomogram of ATG2A and small unilamellar vesicles Method: EM (tomography) EMDB-50659: Cryo-electron tomogram of ATG2A and small unilamellar vesicles Method: EM (tomography) EMDB-50660: Cryo-electron tomogram of ATG2A and small unilamellar vesicles Method: EM (tomography) EMDB-50662: Cryo-electron tomogram of ATG2A and small unilamellar vesicles Method: EM (tomography) EMDB-50666: Cryo-electron tomogram of ATG2A and small unilamellar vesicles Method: EM (tomography) EMDB-50667: Cryo-electron tomogram of ATG2A and small unilamellar vesicles Method: EM (tomography)
Source	homo sapiens (human)
Keywords	LIPID TRANSPORT/MEMBRANE PROTEIN / Lipid transport / ATG2A-WIPI4 complex / single particle cryo-EM / Peripheral membrane proteins / LIPID TRANSPORT-MEMBRANE PROTEIN complex / MEMBRANE PROTEIN / ATG2A / Lipid scramblase / ATG9A / Lipid transfer / ATG9A-ATG2A-WIPI4 complex / autophagy