Arginine‐vasopressin (AVP) regulates water reabsorption in renal collecting duct principal cells. Its binding to Gs‐coupled vasopressin V2 receptors increases cyclic AMP (cAMP) and subsequently elicits the redistribution of the water channel aquaporin‐2 (AQP2) from intracellular vesicles into the plasma membrane (AQP2 shuttle), thereby facilitating water reabsorption from primary urine. The AQP2 shuttle is a paradigm for cAMP‐dependent exocytic processes. Using sections of rat kidney, the AQP2‐expressing cell line CD8, and primary principal cells, we studied the role of the motor protein myosin Vb, its vesicular receptor Rab11, and the myosin Vb‐ and Rab11‐binding protein Rab11‐FIP2 in the AQP2 shuttle. Myosin Vb colocalized with AQP2 intracellularly in resting and at the plasma membrane in AVP‐treated cells. Rab11 was found on AQP2‐bearing vesicles. A dominant‐negative myosin Vb tail construct and Rab11‐FIP2 lacking the C2 domain (Rab11‐FIP2‐ΔC2), which disrupt recycling, caused condensation of AQP2 in a Rab11‐positive compartment and abolished the AQP2 shuttle. This effect was dependent on binding of myosin Vb tail and Rab11‐FIP2‐ΔC2 to Rab11. In summary, we identified myosin Vb as a motor protein involved in AQP2 recycling and show that myosin Vb‐ and Rab11‐FIP2‐dependent recycling of AQP2 is an integral part of the AQP2 shuttle.