(Macro-)Autophagy describes a process responsible for the degradation of intracellular proteins and organelles.In recent years, the ULK1/2 complex comprising the kinase ULK1/2 and the accessory proteins ATG13, RB1CC1 and ATG101 has been identified as central player in the autophagy network.The ULK1 complex is constitutively assembled independent of nutrient supply, and its activation upon starvation is mainly controlled by the dissociation of the mechanistic target of rapamycin complex 1 (MTORC1) and subsequent ULK1/2-mediated autophosphorylation and transphosphorylation of ATG13 and RB1CC1.Here we report the identification of the minimal ATG13 region required for the binding of ULK1/2.The binding site is established by the last three amino acids TLQ of ATG13.This tripeptide motif is essential for the recruitment of ULK1 into the autophagy-initiating high-molecular weight complex.Expression of an ULK1/2 binding-deficient variant in ATG13-deficient cells resulted in diminished but not completely abolished autophagic flux.Collectively, we propose that autophagy can be executed by mechanisms that are dependent or independent of the ULK1/2-ATG13 interaction.