Negative stain transmission electron microscopy (NS-EM) was used to characterize the ATG9A-2A complex. ![]() Mutational analyses combined with functional activity assays demonstrate their importance for autophagy, thereby shedding light on this protein complex at the heart of autophagy. ![]() Using this integrative structure modeling approach, we identify several interfaces mediating ATG9A-2A interaction that would allow a direct transfer of lipids from ATG2A into the lipid-binding perpendicular branch of ATG9A. By combining data from peptide arrays, crosslinking, and hydrogen-deuterium exchange mass spectrometry together with cryoelectron microscopy, we propose a molecular model of the ATG9A-2A complex. Although both have been functionally linked during the formation of autophagosomes, the molecular details and consequences of their interaction remain unclear. ATG9A is a lipid scramblase that allows equilibration of lipids across a membrane bilayer, whereas ATG2A facilitates lipid flow between tethered membranes. ATG9A and ATG2A are essential core members of the autophagy machinery.
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