Canonically, LC3 lipidation has been associated with autophagy pathways but it becomes increasingly clear that this modification can also occur during autophagy‐unrelated processes. In this issue, Florey and colleagues find that the WD40 domain of ATG16L1 is dispensable for LC3 lipidation during starvation‐induced autophagy but required for its lipidation during several other membrane‐based processes that are different from autophagy. This finding opens the door for the analysis of the functions of LC3 lipidation in these pathways.
See also: K Fletcher et al
Macroautophagy (hereafter autophagy) is a process for the delivery of intracellular material, referred to as cargo, into the lysosome for degradation. Autophagy can be triggered by starvation or the presence of intracellular cargoes and entails the de novo formation of a double‐membrane organelle termed autophagosome, within which the cargo is sequestered. During the canonical form of autophagy, a number of conserved AuTophaGy (ATG)‐related proteins act in a hierarchical manner to mediate the formation of autophagosomes. A hallmark of this process is the covalent attachment of ATG8 family proteins (here referred to as LC3) to the membrane lipid phosphatidylethanolamine (PE) on the nascent autophagosomal membrane. This lipidation reaction occurs analogous to the attachment of ubiquitin to target proteins and is mediated by the E1‐like enzyme ATG7 and the E2‐like enzyme ATG3. In addition, a protein complex composed of the …
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