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Speaker: Professor Sharon Tooze, Group Leader, Molecular Cell Biology of Autophagy Laboratory, the Francis Crick Institute
Host: Jody Rosenblatt
Autophagy is a catabolic mechanism by which intracellular cargo, such as long-lived proteins, organelles, aggregates, and intracellular pathogens, are turned over in the lysosome. It involves the de novo formation of a double membraned organelle termed an autophagosome which captures intracellular cargo for delivery to the lysosome. Autophagosome formation can be induced by a host of stimuli, including amino acid starvation. One of the key signalling complexes in autophagy initiation is the serine/threonine kinase ULK complex. ULK1 and the closely related ULK2 are mammalian homologs of yeast Atg1, kinases from both organisms similarly positioned upstream in the autophagic signalling cascade. To better understand ULK1/2 function phosphoproteomic screens were done to identify novel ULK substrates. We focus on one, VPS15, a subunit of the VPS34 class III lipid kinase complex, and a second novel substrate WIPI2. Both the VPS34 complex and WIPI2 are key autophagy proteins in the early stages of the formation of the autophagosome.