Autophagy-related protein 16-1 (ATG16L1)

Autophagy-related protein 16-1 (ATG16L1) is a key scaffold protein required for the formation of autophagosomes during autophagy, the main cellular pathway for degradation of cytoplasmic constituents, damaged organelles, and invading pathogens[1][2][4]. ATG16L1 forms a complex with ATG5 and ATG12, acting as a molecular scaffold to mediate protein-protein and protein-lipid interactions regulating autophagosome formation and vesicle trafficking[2][4]. The protein contains an N-terminal ATG5-binding domain, a central coiled-coil domain responsible for dimerization and complex assembly, and a C-terminal WD40-repeat domain that mediates additional protein interactions[1][2][4]. ATG16L1 is essential for canonical autophagy in all cell types and is also involved in non-canonical functions such as secretion of hormones and immune cell antigen presentation[3][4]. Genetic variations in ATG16L1, especially the T300A variant, are strongly associated with altered susceptibility to Crohn’s disease, highlighting its role in intestinal homeostasis and mucosal immunity[1]. Dysregulation of ATG16L1 is implicated in infection, inflammation, and possibly neurodegeneration and cancer due to its central role in cellular quality control pathways[1][2]. Direct pharmacological modulation of ATG16L1 is not currently available, but it remains a major focus as a potential drug target for diseases involving defective autophagy or immune dysregulation.

Other names

ATG16L1Autophagy-related 16 like 1APG16LWDR30FLJ10035ATG16AIBD10APG16L betaUNQ9393/PRO34307WD repeat domain 30

Not applicable (no direct-acting drugs); indirect mechanisms include modulation of autophagy pathway, immune modulation via autophagy alteration