Kuninori Suzuki

Abstract Autophagy requires de novo autophagosome formation, which depends on supplying millions of phospholipids from membrane-source organelles. In Saccharomyces cerevisiae, Atg2, a lipid transfer protein (LTP), collaborates with the phosphoinositide-binding protein Atg18 in this process. However, it remains largely unknown how the Atg2-Atg18 complex achieves bulk lipid transport and how much it contributes to autophagosome biogenesis.

Structural Basis of the Propeptide-Mediated Formation of the Ape1 Complex Atg19 Binding Inhibits the prApe1 Aggregation by Competing with Propeptide Self-Assembly Atg19 Regulates the Size of the Ape1 Complex Optimal as a Selective Cargo It is known that the diameter of Cvt vesicles is consistently 150 nm, which contrasts with the various sizes (300–900 nm) of starvation-induced autophagosomes (Baba et al., 1994xUltrastructural analysis of the autophagic process in yeast: detection of...