The year 2013 marked the 50th anniversary of C de Duve's coining of the term "autophagy" for the degradation process of cytoplasmic constituents in the lysosome/vacuole. This year, de Duve passed away, leaving a legacy in autophagy research. After the discovery of lysosomes, electron microscopy revealed autophagy as a means of delivering intracellular components to the lysosome. For many years, molecular understanding of autophagy was limited. The first breakthrough came in the 1990s when autophagy was observed in yeast under starvation. Genetic studies led to the discovery of autophagy-defective mutants, and the identification of autophagy-related genes in yeast revealed unique molecules involved in autophagy. ATG homologs were found in various organisms, indicating that autophagy mechanisms are conserved among eukaryotes. These findings revolutionized autophagy research, leading to significant progress in understanding its molecular mechanisms, physiological roles, and relevance to health and disease. Autophagy is a process by which cells degrade their own components, involving the formation of autophagosomes that fuse with lysosomes. The discovery of lysosomes by de Duve led to the identification of autophagy as a process of delivering cytoplasmic materials to lysosomes for degradation. Autophagy was defined by de Duve in 1963 as "self-eating," contrasting with "heterophagy" (endocytosis). Autophagy plays a crucial role in protein turnover, especially under starvation conditions. It is tightly regulated by nutrient conditions and involves the degradation of long-lived proteins. Autophagy is also involved in the control of organelle quantity and the selective degradation of organelles. The study of autophagy faced challenges due to the lack of specific markers and the transient nature of autophagosomes. However, the discovery of yeast as a model organism led to the identification of autophagy-related genes (ATG genes). Genetic analysis of yeast revealed that autophagy is essential for survival during starvation. The discovery of ATG genes in yeast and their homologs in other organisms has greatly advanced the understanding of autophagy. The identification of ATG genes in mammals and other organisms has shown that autophagy mechanisms are conserved across eukaryotes. The study of autophagy has led to the identification of various conjugation systems, such as the Atg12 conjugation system and the Atg8 lipidation system, which are essential for autophagosome formation. The discovery of these systems has provided insights into the molecular mechanisms of autophagy and its role in cellular processes. The development of genetic tools and models has enabled the study of autophagy in mammals, leading to the identification of key genes and pathways involved in autophagy. The understanding of autophagyThe year 2013 marked the 50th anniversary of C de Duve's coining of the term "autophagy" for the degradation process of cytoplasmic constituents in the lysosome/vacuole. This year, de Duve passed away, leaving a legacy in autophagy research. After the discovery of lysosomes, electron microscopy revealed autophagy as a means of delivering intracellular components to the lysosome. For many years, molecular understanding of autophagy was limited. The first breakthrough came in the 1990s when autophagy was observed in yeast under starvation. Genetic studies led to the discovery of autophagy-defective mutants, and the identification of autophagy-related genes in yeast revealed unique molecules involved in autophagy. ATG homologs were found in various organisms, indicating that autophagy mechanisms are conserved among eukaryotes. These findings revolutionized autophagy research, leading to significant progress in understanding its molecular mechanisms, physiological roles, and relevance to health and disease. Autophagy is a process by which cells degrade their own components, involving the formation of autophagosomes that fuse with lysosomes. The discovery of lysosomes by de Duve led to the identification of autophagy as a process of delivering cytoplasmic materials to lysosomes for degradation. Autophagy was defined by de Duve in 1963 as "self-eating," contrasting with "heterophagy" (endocytosis). Autophagy plays a crucial role in protein turnover, especially under starvation conditions. It is tightly regulated by nutrient conditions and involves the degradation of long-lived proteins. Autophagy is also involved in the control of organelle quantity and the selective degradation of organelles. The study of autophagy faced challenges due to the lack of specific markers and the transient nature of autophagosomes. However, the discovery of yeast as a model organism led to the identification of autophagy-related genes (ATG genes). Genetic analysis of yeast revealed that autophagy is essential for survival during starvation. The discovery of ATG genes in yeast and their homologs in other organisms has greatly advanced the understanding of autophagy. The identification of ATG genes in mammals and other organisms has shown that autophagy mechanisms are conserved across eukaryotes. The study of autophagy has led to the identification of various conjugation systems, such as the Atg12 conjugation system and the Atg8 lipidation system, which are essential for autophagosome formation. The discovery of these systems has provided insights into the molecular mechanisms of autophagy and its role in cellular processes. The development of genetic tools and models has enabled the study of autophagy in mammals, leading to the identification of key genes and pathways involved in autophagy. The understanding of autophagy