RAB24 is an atypical member of the RAB GTPase family with distinct regulatory roles in autophagy and cellular metabolism. Unlike conventional RAB proteins, RAB24 exhibits low intrinsic GTPase activity and exists predominantly in the GTP-bound active state 1. The protein is required for clearance of late autophagic vacuoles under basal conditions but is not essential for starvation-induced autophagy 12. RAB24 demonstrates unique subcellular localization, being predominantly nuclear in COS-7 cells and interacting with cyclophilin A and GABARAP 3. Importantly, RAB24 undergoes tyrosine phosphorylation by Src-family kinases, making it the first reported tyrosine-phosphorylated member of the Ras superfamily 4. In hepatic metabolism, RAB24 controls mitochondrial fission and is upregulated in NAFLD patients, with liver-specific inhibition improving hepatic steatosis and glucose homeostasis 5. RAB24 shows tissue-specific expression patterns with highest levels in brain and kidney, and dynamic developmental changes 6. Disease associations include hereditary ataxia in dogs caused by RAB24 mutations affecting Purkinje neurons 7, and elevated expression in hepatocellular carcinoma correlating with poor prognosis 8. These findings establish RAB24 as a multifunctional regulator linking intracellular trafficking to metabolic homeostasis and disease pathogenesis.