Aquaporin2 (AQP2) is a key water channel in kidney collecting duct cells, regulated mainly by vasopressin through both cAMP-dependent and independent pathways (1, 4). Phosphorylation at Ser256 is essential for AQP2 membrane targeting, while Ser269 stabilizes it (3). Recent research suggests that cAMP-independent mechanisms also regulate AQP2 trafficking, challenging traditional models (4). Additionally, LRBA has been identified as a crucial protein for AQP2 phosphorylation and urinary concentration (2). Post-translational modifications such as ubiquitination and glycosylation further influence AQP2 stability and function (3). These insights have significant implications for treating water balance disorders, such as nephrogenic diabetes insipidus (1, 2).