Dataset Information


The WD40 domain of ATG16L1 is required for its non-canonical role in lipidation of LC3 at single membranes.

ABSTRACT: A hallmark of macroautophagy is the covalent lipidation of LC3 and insertion into the double-membrane phagophore, which is driven by the ATG16L1/ATG5-ATG12 complex. In contrast, non-canonical autophagy is a pathway through which LC3 is lipidated and inserted into single membranes, particularly endolysosomal vacuoles during cell engulfment events such as LC3-associated phagocytosis. Factors controlling the targeting of ATG16L1 to phagophores are dispensable for non-canonical autophagy, for which the mechanism of ATG16L1 recruitment is unknown. Here we show that the WD repeat-containing C-terminal domain (WD40 CTD) of ATG16L1 is essential for LC3 recruitment to endolysosomal membranes during non-canonical autophagy, but dispensable for canonical autophagy. Using this strategy to inhibit non-canonical autophagy specifically, we show a reduction of MHC class II antigen presentation in dendritic cells from mice lacking the WD40 CTD Further, we demonstrate activation of non-canonical autophagy dependent on the WD40 CTD during influenza A virus infection. This suggests dependence on WD40 CTD distinguishes between macroautophagy and non-canonical use of autophagy machinery.

PROVIDER: S-EPMC5813257 | BioStudies |

REPOSITORIES: biostudies

Similar Datasets

| S-EPMC7032593 | BioStudies
| S-EPMC5563147 | BioStudies
| S-EPMC4899871 | BioStudies
2017-01-01 | S-EPMC5446083 | BioStudies
| S-EPMC8567314 | BioStudies
| S-EPMC6377711 | BioStudies
| S-EPMC7604492 | BioStudies
| S-EPMC6484409 | BioStudies
| S-EPMC7679444 | BioStudies
| S-EPMC5486363 | BioStudies