Rab10

Rab10 is a member of the Rab family of small GTPases that regulate vesicular trafficking in eukaryotic cells. It is encoded by the RAB10 gene in humans. Like other Rab proteins, Rab10 cycles between a GTP-bound active state and a GDP-bound inactive state and is typically anchored to membranes through a C-terminal prenylation motif.

Rab10 localizes primarily to the trans-Golgi network and recycling endosomes, and to vesicles en route to the plasma membrane. Through these compartments, it participates in sorting and trafficking events between the Golgi, endosomal system, and the plasma membrane. In polarized epithelial cells, Rab10 contributes to basolateral sorting, supporting directional trafficking within the cell.

In adipocytes and muscle cells, Rab10 participates in the insulin-stimulated translocation of GLUT4-containing vesicles to the plasma membrane, thereby promoting glucose uptake. Its activity is regulated by factors that control the GDP/GTP cycle, as well as various effector proteins that mediate vesicle movement, docking, and fusion.

In human disease research, Rab10 is a substrate of the LRRK2 kinase, and phosphorylation of Rab10 is used as a readout of LRRK2 activity in Parkinson’s disease models. Altered Rab10 function or regulation can perturb endolysosomal trafficking and membrane recycling, which has drawn interest in neurodegenerative disease contexts.

Rab10 is broadly conserved across eukaryotes and is widely expressed, reflecting its general role in membrane trafficking. As with other Rab proteins, its precise functions can vary by cell type and physiological conditions, and ongoing studies continue to clarify its interactors and regulatory networks.