RAB2A is a small GTPase that regulates intracellular membrane trafficking by cycling between active GTP-bound and inactive GDP-bound states 1. Its primary function involves coordinating multiple trafficking pathways essential for cellular homeostasis. RAB2A regulates autophagy by promoting autophagosome-lysosome fusion through recruitment of the HOPS endosomal tethering complex, where autophagosomal RAB2A and lysosomal RAB39A coordinately recruit distinct HOPS subcomplexes to mediate membrane tethering and fusion 1. RAB2A also functions in early autophagy by facilitating ULK1 complex recruitment to phagophores and modulating ULK1 kinase activity 2. Additionally, RAB2A is required for protein transport from the endoplasmic reticulum to the Golgi complex and regulates Golgi morphology 3, while mediating unconventional protein secretion via the ERGIC compartment 4. Beyond autophagy, RAB2A regulates VLDL secretion in hepatocytes by mediating lipid droplet-Golgi interactions through interaction with HSD17B13 5. Its activity is suppressed by AMPK-dependent pathways 5, and TBC1D4 serves as a negative regulator antagonizing both autophagic and endocytic RAB2A functions 6. In cancer, RAB2A promotes metastatic dissemination by controlling E-cadherin and MT1-MMP trafficking 7. RAB2A has also been identified as a host factor required for COVID-19 critical illness 8.