Covalent conjugation of ATG12 to the lysine 130 residue (K130) of ATG5 is followed by the addition of ATG16L
protein to the complex.
Zhang et al., "HucMSC exosomes-delivered 14-3-3[zeta] enhanced autophagy via modulation of ATG16L
in preventing cisplatin-induced acute kidney injury," American Journal of Translational Research, vol.
This complex finally associates with ATG16L
. LC-3, the mammalian homologue of ATG-8 in yeast, undergoes an ATG-4-mediated proteolytic cleavage resulting in the formation of LC-3I, a cytosolic form able to bind ATG-7, subsequently conjugated by ATG-3 (E2-like ubiquitin carrier) to phosphatidylethanolamine (PE) so as to generate LC-3II.
The incorporation of LC3 into autophagosomes is also mediated by the ATG5/ATG12 complex, which, together with ATG16L, forms a new complex that functions similarly to an E3 enzyme .
ATG16L relocalizes at the basal body of the PC in conditions of serum starvation or when ciliary Hh signaling is increased.
Furthermore, the phagophore expands after conjugation of ATG12 to ATG5 which interacts with ATG16 forming the ATG16L complex which then conjugates phosphatidylethanolamine (PE) to the procures of microtubule-associated protein 1 light chain 3 (LC3) until generation of the LC3 II receptor.
The phagophore is elongated by the autophagy proteins ATG12-ATG5 creating the ATG16L complex, which then conjugates phosphatidylethanolamine (PE) to the procures of microtubule-associated protein 1 Light Chain 3 (LC3) to generate the LC3 II receptor.
The Atg12-Atg5 conjugate then interacts with Atg16L to form the Atg5-Atg12-Atg16L complex.
Yoshimori, "The Atg16L complex specifies the site of LC3 lipidation for membrane biogenesis in autophagy," Molecular Biology of the Cell, vol.