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. 2023 Feb 9;14(9):632–634. doi: 10.1093/procel/pwad005

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©The Author(s) 2023. Published by Oxford University Press on behalf of Higher Education Press.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 1. — ORP8 acts as the receptor for autophagic turnover of lipid droplets. ORP8 is localized on the lipid droplets (LDs) via its C-terminal transmembrane (TM) domain. Upon lipophagy induction, for example, by oleic acid (OA) treatment or starvation, ORP8 on LDs interacts with LC3/GABARAPs, thus acting as a receptor to mediate the delivery of LDs to the lysosome for degradation to release free fatty acids (FFAs). Three LIR motifs within the PH domain mediate the binding of ORP8 to LC3/GABARAPs upon lipophagy induction. This binding is facilitated by AMPK-mediated phosphorylation at the Thr54 and Ser65 sites of ORP8.