Ralph Hardenberg

TL;DR: Light is shed in the interrelationship between Atg9, Atg2, and Atg18 and the possible functional relevance of the phagophore–ER contact sites in phagophile expansion is highlighted.

TL;DR: The authors showed that Atg8-phosphatidylethanolamine pool essential for autophagosome formation is protected at least in part by Atg4 phosphorylation by Atga1 while newly synthesized cytoplasmic Atga8 remains susceptible to constitutive Atga4 processing.

TL;DR: This work shows that yeast Atg4 is recruited onto autophagosomal membranes by direct binding to Atg8 via two evolutionarily conserved At g8 recognition sites, a classical LC3‐interacting region (LIR) at the C‐terminus of the protein and a novel motif at the N‐ terminus.

TL;DR: In this article , Atg9 function is dramatically compromised by a F627A mutation within the conserved interface between the transmembrane domains of the ATg9 monomers.

TL;DR: The observations suggest that Bph1 is a novel Rab5 effector that maintains endosomal functioning, and Atg8 is lipidated at endosomes even during normal growth and ends up in the vacuole lumen.