RAB32 is a small GTPase that regulates intracellular membrane trafficking by cycling between inactive GDP-bound and active GTP-bound states, recruiting downstream effectors responsible for vesicle formation, movement, tethering, and fusion. Beyond vesicular transport, RAB32 serves as an A-kinase anchoring protein that localizes protein kinase A to the mitochondrion and coordinates mitochondrial fission dynamics. RAB32 plays critical roles in phagosome maturation against pathogens such as Salmonella and Mycobacterium tuberculosis, and controls melanin production through proper trafficking of melanogenic enzymes to melanosomes. Recent evidence links RAB32 variants to human disease. The RAB32 c.213C>G (Ser71Arg) variant segregates with autosomal dominant Parkinson's disease in multiple families and shows significant association with idiopathic Parkinson's disease (odds ratio 13.17, 95% CI 2.15–87.23; p=0.0055) 1. In functional assays, RAB32 Arg71 activates LRRK2 kinase more efficiently than wild-type RAB32 1, suggesting shared mechanisms with other genetically inherited forms of parkinsonism. In glioblastoma, elevated RAB32 expression correlates with poor prognosis and aggressive phenotypes; RAB32 regulates ERK1/2-dependent mitochondrial fission through Drp1 recruitment, driving mesenchymal transition and invasion 2. Elevated RAB32 expression has also been detected in chr6 obstructive pulmonary disease lung tissues 3.