The biogenesis of endosomes and lysosomes is tightly connected to several membrane trafficking pathways from the Golgi or the plasma membrane. In addition, autophagosomes deliver organelles or misfolded proteins via double membrane vesicles to the lysosome. For the final fusion of late endosomes and autophagosomes with the lysosome, these organelles require the right membrane code. Lipids such as phosphatidylinositol phosphates, and here in particular PI(3)P, and the Rab7 GTPases are most critical. These are recognized by peripheral membrane proteins involved in tethering and membrane fusion such as the HOPS tethering complex. On yeast lysosomes, also called vacuoles, Rab7 activity is controlled by the activating GEF Mon1-Ccz1 and the counteracting GAP Gyp7, whereas PI(3)P levels are controlled by the lipid kinase Vps34 and the myotubularin phosphatase Ymr1, and the PIKfyve lipid kinase. How each of these membrane codes are generated, controlled in their abundance, and contribute to membrane homeostasis of the lysosome, is still largely unclear. Within my lecture, I will provide recent insights into our current understanding of the role of the yeast Rab7 Ypt7 protein and the lipid modifying machineries in lysosomal membrane homeostasis. I will further discuss the possible mechanisms how membrane fusion and fission at the yeast lysosome is coordinated with cellular stress and physiology.