RAB10 is a member of the RAS oncogene family that functions as a GTPase involved in membrane trafficking and cellular transport processes. RAB10 serves as a direct substrate of LRRK2 kinase, becoming phosphorylated at threonine-73 (pT73), which regulates its activity and subcellular localization 12. The protein localizes to various cellular compartments including the endoplasmic reticulum, lysosomes, and trans-Golgi network, with phosphorylated RAB10 showing enrichment at presynaptic terminals 2. RAB10 plays critical roles in lysosomal function, particularly in LRRK2-mediated lysosomal tubulation and vesicle sorting processes 34. The protein also facilitates intraluminal vesicle transport to migrasomes through interaction with Caveolin-1 and Myosin Va 5. In disease contexts, RAB10 is implicated in Parkinson's disease pathogenesis, where hyperactive LRRK2 causes excessive RAB10 phosphorylation, leading to lysosomal dysfunction 67. Additionally, RAB10 contributes to bacterial invasion mechanisms, as Salmonella exploits LRRK2-dependent RAB10 phosphorylation to generate membrane reservoirs that facilitate cellular invasion 8. RAB10 deficiency produces distinct effects on lysosomal pH and protein aggregation patterns in human neurons 7.