The article reviews the molecular mechanisms of autophagy, a fundamental process in eukaryotic cells that involves the formation of double-membrane-bound compartments to sequester and degrade cytoplasmic components. Autophagy was first discovered in yeast and has since been extensively studied, leading to the identification of genes and proteins involved in this process. The core Atg proteins, including the Atg1 kinase complex, the phosphatidylinositol 3-kinase complex, the Atg12 conjugation system, and the Atg8 conjugation system, play crucial roles in the formation of autophagosomal membranes. Recent studies have revealed dynamic aspects of the pre-autophagosomal structure (PAS), which is essential for autophagosome formation. The PAS is a dynamic assembly of core Atg proteins and 'conductor' proteins that regulate the spatiotemporal organization of the core proteins. The Atg17-Atg29-Atg31 complex acts as a conductor, while the Atg1-Atg13 complex is involved in the initial steps of autophagosome formation. The Atg12-Atg5-Atg16 complex has an E3-like function in the lipidation of Atg8. The article also discusses the role of Atg8 in selective autophagy and the dynamic features of the PAS. Overall, the review highlights the conservation of autophagy mechanisms from yeast to higher eukaryotes and the importance of understanding these mechanisms for both physiological and pathological processes.The article reviews the molecular mechanisms of autophagy, a fundamental process in eukaryotic cells that involves the formation of double-membrane-bound compartments to sequester and degrade cytoplasmic components. Autophagy was first discovered in yeast and has since been extensively studied, leading to the identification of genes and proteins involved in this process. The core Atg proteins, including the Atg1 kinase complex, the phosphatidylinositol 3-kinase complex, the Atg12 conjugation system, and the Atg8 conjugation system, play crucial roles in the formation of autophagosomal membranes. Recent studies have revealed dynamic aspects of the pre-autophagosomal structure (PAS), which is essential for autophagosome formation. The PAS is a dynamic assembly of core Atg proteins and 'conductor' proteins that regulate the spatiotemporal organization of the core proteins. The Atg17-Atg29-Atg31 complex acts as a conductor, while the Atg1-Atg13 complex is involved in the initial steps of autophagosome formation. The Atg12-Atg5-Atg16 complex has an E3-like function in the lipidation of Atg8. The article also discusses the role of Atg8 in selective autophagy and the dynamic features of the PAS. Overall, the review highlights the conservation of autophagy mechanisms from yeast to higher eukaryotes and the importance of understanding these mechanisms for both physiological and pathological processes.