RAB36 is a small GTPase member of the Rab family that regulates intracellular membrane trafficking by cycling between inactive GDP-bound and active GTP-bound states 1. The protein localizes to the Golgi apparatus and regulates the spatial distribution of late endosomes and lysosomes through interaction with the effector protein RILP, operating via a mechanism similar to the related protein Rab34 2. RUTBC2 functions as a GTPase-activating protein (GAP) for Rab36, linking Rab9A-mediated mannose 6-phosphate receptor recycling to Rab36 function in the endosomal system 3. In disease contexts, RAB36 has been implicated in cancer progression. MicroRNA-mediated downregulation of RAB36 suppresses bladder cancer cell proliferation and invasion 4, while circular RNA-mediated sequestration of regulatory factors that suppress RAB36 promotes colorectal cancer liver metastasis 5. Additionally, a genome-wide association study identified a locus near RAB36 associated with trait resilience, suggesting potential psychiatric relevance 6. RAB36 is also targeted by the Chlamydia pneumoniae pathogenic protein Mbp1, which recruits Rab36 to bacterial inclusions 7.