Tetsuya Kotani

TL;DR: Structural and biochemical data suggest that the essential autophagy protein Atg2 acts as a lipid-transfer protein that supplies phospholipids from the source organelle to the isolation membranes (IMs) for autophagosome formation.

TL;DR: It is reported that yeast and human Atg9 are lipid scramblases that translocate phospholipids between outer and inner leaflets of liposomes in vitro, thereby driving autophagosomal membrane expansion.

TL;DR: Atg2 has two membrane-binding domains in the N- and C-terminal regions and acts as a membrane tether during autophagosome formation in the budding yeast Saccharomyces cerevisiae, and it is proposed that the Atg2-Atg18 complex tethers the PAS to the ER to initiate membrane expansion during autophileagosomes formation.

TL;DR: A novel mechanism for the PAS targeting of Atg12-Atg5- atg16 is discovered, which is mediated by the interaction of AtG12 with the Atg1 kinase complex that serves as a scaffold for PAS organization.

TL;DR: It is revealed that the nuclear pore complex and nucleoporins are degraded by selective autophagy upon inactivation of Tor kinase complex 1 in Saccharomyces cerevisiae.