Glucose starvation can activate cellular autophagy, but the exact mechanisms of this have been unclear. PhD student Cansu Karabiyik and colleagues from the Rubinsztein lab have recently uncovered a phosphorylation pathway involving both proteins and lipids which casts new light on this important regulatory process. Their publication in Developmental Cell shows how AMP-activated protein kinase, a sensor of cellular energy levels, activates the protein kinase ULK1, which, in turn, activates the lipid kinase PIKfyve on recycling endosomes. The resultant PI(5)P lipid then plays a role in recruiting proteins key to the biogenesis of autophagosomes. This newly-discovered pathway is distinct from canonical autophagosome generation which requires the lipid PI(3)P.