The study investigates the role of Rab11 in the recycling endosome, a key component in membrane traffic. Rab11 was found to colocalize with internalized transferrin in the pericentriolar recycling compartment of CHO and BHK cells. Overexpression of Rab11 mutants, particularly those in the GDP-bound state, altered the morphology of the recycling endosome and inhibited recycling of transferrin from this compartment. The early endocytic regulator Rab5 acted before Rab11 in the transferrin recycling pathway, as its expression prevented transport to the Rab11-positive recycling endosome. These findings suggest that Rab11 plays a novel role in controlling traffic through the recycling endosome, acting distal to Rab5 in the endocytic pathway.The study investigates the role of Rab11 in the recycling endosome, a key component in membrane traffic. Rab11 was found to colocalize with internalized transferrin in the pericentriolar recycling compartment of CHO and BHK cells. Overexpression of Rab11 mutants, particularly those in the GDP-bound state, altered the morphology of the recycling endosome and inhibited recycling of transferrin from this compartment. The early endocytic regulator Rab5 acted before Rab11 in the transferrin recycling pathway, as its expression prevented transport to the Rab11-positive recycling endosome. These findings suggest that Rab11 plays a novel role in controlling traffic through the recycling endosome, acting distal to Rab5 in the endocytic pathway.