This study demonstrates a novel pathway for autophagy induction in yeast cells under endoplasmic reticulum (ER) stress conditions. ER stress, caused by the accumulation of misfolded proteins, activates the unfolded protein response (UPR) to induce the expression of chaperones and proteins involved in recovery. The study shows that ER stress stimulates the assembly of the pre-autophagosomal structure (PAS) and promotes autophagosome formation and transport to the vacuole in an Atg protein-dependent manner. Atg1 kinase activity, which reflects both nutritional status and autophagic state, was found to be high during ER stress-induced autophagy. These findings indicate that ER stress can induce autophagy, providing a new mechanism for cellular stress response. The study also highlights the role of Atg1 kinase in this process and suggests that ER stress may act through a different pathway from the typical nutrient starvation-induced autophagy.This study demonstrates a novel pathway for autophagy induction in yeast cells under endoplasmic reticulum (ER) stress conditions. ER stress, caused by the accumulation of misfolded proteins, activates the unfolded protein response (UPR) to induce the expression of chaperones and proteins involved in recovery. The study shows that ER stress stimulates the assembly of the pre-autophagosomal structure (PAS) and promotes autophagosome formation and transport to the vacuole in an Atg protein-dependent manner. Atg1 kinase activity, which reflects both nutritional status and autophagic state, was found to be high during ER stress-induced autophagy. These findings indicate that ER stress can induce autophagy, providing a new mechanism for cellular stress response. The study also highlights the role of Atg1 kinase in this process and suggests that ER stress may act through a different pathway from the typical nutrient starvation-induced autophagy.