RAB6A is a small GTPase that regulates intracellular membrane trafficking by cycling between inactive GDP-bound and active GTP-bound conformations to recruit effector proteins 1. As a key regulator of COPI-independent retrograde transport, RAB6A mediates vesicle movement from the Golgi apparatus toward the endoplasmic reticulum and recruits VPS13B to Golgi membranes 12. RAB6A contains a low intrinsic GTPase activity and functions through dynein-dependent mechanisms requiring the adaptor BICD2 34. In neural development, RAB6A operates within a RAB6-dynein-LIS1 complex essential for post-Golgi apical transport of the determinant Crumbs3. Double knockout of RAB6A/A' impairs apical localization and causes radial glial cell delamination, disrupting neuroepithelial integrity 3. RAB6A exhibits functional differentiation from its isoform RAB6A', with RAB6A' primarily mediating retrograde transport while RAB6A appears less critical for standard trafficking 5. RAB6A serves as a pan-astrocytic marker abundantly expressed in peripheral astrocyte processes 6. Clinically, RAB6A dysregulation promotes cancer stem cell properties in cholangiocarcinoma by modulating osteopontin secretion and activating AKT signaling 7. RAB6A is also hijacked by human papillomavirus for nuclear trafficking during viral entry 4, suggesting therapeutic potential in targeting this pathway.