WDR7 (WD repeat domain 7) is a cytoplasmic protein essential for V-ATPase assembly and regulation of organellar acidification. WDR7 functions as a core component of the metazoan RAVE (regulator of H+-ATPase) complex, assembling with DMXL1/DMXL2 and ROGDI to facilitate V1-VO association and enable proton pumping into lysosomes and synaptic vesicles 1. This RAVE complex is recruited to lysosomes upon TRPML1 activation in a CASM-dependent manner, promoting V1-ATPase subunit recruitment and maintaining proper lysosomal pH and hydrolytic capacity 2. WDR7 also regulates dense-core vesicle acidification by interacting with CAPS1 and DMXL2, supporting neurotransmitter loading and hormonal processing 3. Beyond organellar function, WDR7 serves as a host dependency factor for viral replication. It is essential for influenza A virus entry and V-ATPase regulation 4, and critical for replication of bunyaviruses including Rift Valley fever phlebovirus and La Crosse encephalitis virus 56. Clinically, WDR7 variants associate with metabolic and neurological disease. Intronic WDR7 variants are associated with fasting insulin levels and type 2 diabetes risk 7, and WDR7 is identified as a candidate ALS-associated gene 8, suggesting dysfunction in V-ATPase assembly may contribute to motor neuron pathology.