Figure 2
From: Regulation of autophagy by protein post-translational modification
Phosphorylation of autophagy proteins. Under normal conditions, the phosphorylated active MTORC1 complex interacts with and inhibits the ULK1/ATG1 complex. Following autophagy induction in response to starvation, or rapamycin exposure, the MTORC1 complex releases the ULK1/ATG1 complex leading to its activation and its auto-phosphorylation on ULK1, FIP200, and ATG13 (1). The ULK1 complex then recruits the PI3KIII complex to induce the formation of the phagophore (2). This step is also regulated by the BECN1/ATG6–BCL2 interaction and the JNK1 kinase (3). Upstream AMPK activates (4), and AKT inhibits (5), the autophagy process. ATG9 (6) and LC3 (7) are also regulated by phosphorylation.
