RAB41 is a small GTPase member of the Rab protein family that functions as a key regulator of intracellular membrane trafficking 1. As a GTPase, RAB41 cycles between inactive GDP-bound and active GTP-bound states to recruit downstream effectors responsible for vesicle formation, movement, tethering, and fusion 1. RAB41 is specifically required for normal Golgi ribbon organization and ER-to-Golgi trafficking 1. RAB41 depletion scatters the Golgi ribbon into isolated punctate elements and impairs VSV-G protein transport from the ER to Golgi 1. Unlike related Rab6 proteins, RAB41 uniquely affects Golgi structure through a contrasting mechanism involving regulation of minus- and plus-end directed motor protein recruitment 2. Beyond canonical trafficking, RAB41 has emerged as a critical component in cellular defense mechanisms. The protein relocates from the Golgi to bacterial-containing autophagic vesicles during Streptococcus pneumoniae infection, where it facilitates selective autophagy and bacterial elimination 3. RAB41 also recruits ESCRT machinery to damaged xenophagolysosomes via a GTPase-independent mechanism mediated by adaptor protein TOM1L2, maintaining membrane homeostasis during bacterial infection 4. Additionally, RAB41 expression is elevated in oral squamous cell carcinoma and promotes cancer cell proliferation and epithelial-mesenchymal transition 5. RAB41 depletion inhibits cell growth, indicating a broader role in cell proliferation 1.