RAB32 is a small GTPase that functions as a molecular switch regulating intracellular membrane trafficking by cycling between inactive GDP-bound and active GTP-bound forms to recruit effector proteins 1. Beyond canonical vesicular trafficking, RAB32 serves as an A-kinase anchoring protein that localizes protein kinase A to mitochondria and regulates Golgi dynamics through PKA-mediated phosphorylation of optineurin 2. RAB32 coordinates critical cellular processes including mitochondrial fission synchronization, melanosome biogenesis, and phagosome maturation for pathogen elimination 3. RAB32 plays a prominent role in cell-autonomous host defense against intracellular bacteria. It facilitates delivery of the antimicrobial metabolite itaconate to pathogen-containing vacuoles through interaction with IRG1 4, restricting replication of Salmonella and Listeria monocytogenes 5. Additionally, RAB32 regulates ERK1/2-dependent Drp1 activation to promote mitochondrial fission, driving glioblastoma migration and invasion through mesenchymal transition 6. Genetically, the RAB32 Ser71Arg variant causes autosomal dominant Parkinson's disease (PARK-RAB32) by hyperactivating LRRK2 kinase 7. Clinically, PARK-RAB32 presents with typical parkinsonism onset around age 54, favorable dopaminergic response, prominent hyposmia, autonomic dysfunction, and evidence of α-synucleinopathy 8. RAB32 dysregulation also associates with chr6 obstructive pulmonary disease pathogenesis 9.