Gastric parietal cells regulate the delivery of the proton pump to the apical lumen by the greatest and most elaborate apical recycling system known in mammalian cells. In the resting state, H/K-ATPase is sequestered inside the cell in tubulovesicular membranes, which fuse with a tortuous intracellular canaliculus in response to secretory stimuli. Moreover, with cessation of secretory stimuli, H/K-ATPase recycles out of the apical plasma membrane and back in tubulovesicles. Investigations over the past 20 years have established the role of the family of Rab11 small GTPases (Rab11a, Rab11b and Rab25) in the regulation of not only parietal cell secretion, but also in general recycling system. Immunoisolation and proteomic characterization of tubulovesicles demonstrated a group of characteristic proteins including Rabs, VAMPs and syntaxins that are candidate regulators of recycling. More recent studies have demonstrated that Rab11a and its effectors, myosin Vb and Rab11-FIPs play broad roles in regulating apical recycling in polarized cells as well as in the development and maintenance of polarity. Alteration of the interactions of Rab11a with both myosin V and Rab11-FIPs leads to both disruption of proper trafficking as well as alterations in junctional composition and even frank loss of polarity and transformation. Thus, proper vesicle trafficking and membrane recycling is critical for the maintenance of membrane polarity and function.