PfATG18 links V-ATPase assembly to endocytic membrane dynamics in malaria parasites.

PfATG18 is essential for V-ATPase stability and vacuolar membrane dynamics, with its loss causing parasite death and vacuole fragmentation in Plasmodium falciparum.

• Why it matters: Understanding how malaria parasites maintain vacuolar homeostasis is crucial for identifying new drug targets, as these processes are vital for parasite survival and drug response.
• What they did: Using genetic manipulation, live-cell imaging, and electron microscopy, researchers identified PfATG18 as a key regulator that interacts with V-ATPase assembly factors and membrane trafficking complexes.
• The result: Disruption of PfATG18 impairs V-ATPase function, leading to defective vacuolar fusion and parasite death, and increases sensitivity of ring-stage parasites to dihydroartemisinin, highlighting its potential as a therapeutic target.