The study investigates the mechanism by which ULK1 kinase induces autophagy through phosphorylation of Beclin-1 and activation of the VPS34 lipid kinase. Upon amino acid starvation or mTOR inhibition, activated ULK1 phosphorylates Beclin-1 at serine 14 (S14), enhancing the activity of ATG14L-containing VPS34 complexes. This phosphorylation is essential for full autophagic induction in mammals and C. elegans. The research reveals a critical link between ULK1 and VPS34 in autophagy induction, highlighting the importance of ULK1 in regulating the autophagy-specific VPS34 complex.The study investigates the mechanism by which ULK1 kinase induces autophagy through phosphorylation of Beclin-1 and activation of the VPS34 lipid kinase. Upon amino acid starvation or mTOR inhibition, activated ULK1 phosphorylates Beclin-1 at serine 14 (S14), enhancing the activity of ATG14L-containing VPS34 complexes. This phosphorylation is essential for full autophagic induction in mammals and C. elegans. The research reveals a critical link between ULK1 and VPS34 in autophagy induction, highlighting the importance of ULK1 in regulating the autophagy-specific VPS34 complex.