Rab35 belongs to the small GTPase superfamily. By interacting with its specific GEF or GAP, Rab35 regulates cargo-specific endocytosis at the vesicle recycling step or mediates exocytosis at the exosome docking/tethering step. During cytokinesis, Rab35 interacts with OCRL phosphatase and is essential for maintaining intercellular bridge stability and abscission by controlling the concentration of phosphatidylinositol 4,5-bisphosphate and SEPT2 localization at the intercellular bridge. Rab35 also plays a role in actin assembly and the recruitment of Cdc42 and Rac1 to the site of filopodium by its direct interaction with actin-bundling protein fascin and actin-binding protein connecdenn 3.
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