Abstract
RAB-11/Rab11 is an endosomal GTPase with conserved roles in directional trafficking and apical domain formation in polarized epithelial cells. From a yeast two-hybrid screen using full-length C. elegans RAB-11 as bait, we identified LEC-5 as a novel binding protein for RAB-11. LEC-5 is an ortholog of mammalian Galectin-9 which associates with glycosphingolipids and is implicated in apical cargo sorting. We further confirmed the interaction between RAB-11 and LEC-5 via GST-pull down, co-immunoprecipitation and bimolecular fluorescence complementation. In addition, we showed that LEC-5 binds to RAB-11 with its C-terminus. Our results indicate a novel role of RAB-11 in apical sorting via LEC-5. Such a role would extend RAB-11's function as a master regulator of apical trafficking and suggest it could translate apical sorting signals into apical vesicle directionality.