We recently reported that ANGII inhibits NBCe1 current and surface expression in Xenopus oocytes. Here we investigated mechanisms of ANGII-induced changes in NBCe1 surface expression. We showed that PKC inhibitor GF109203X blocks and EGTA reduces surface cotransporter loss in ANGII-treated oocytes, suggesting roles for PKC and Ca²⁺. Using endosomal marker FM4-64 and EGFP-tagged NBCe1, we showed that ANGII stimulates endocytosis of NBCe1. To eliminate the possibility that ANGII inhibits NBCe1 recycling, we demonstrated that recycling inhibitor monensin decreases surface expression, accumulates NBCe1-EGFP in endosomes and inhibits NBCe1 current. Monensin and ANGII applied together produce greater inhibition of NBCe1 current than either alone. This additive effect of monensin and ANGII suggests that ANGII stimulates internalization of NBCe1. We used calmodulin antagonist W13, which controls recycling by blocking the exit of the endocytosed cargo from early endosomes, to determine CaM role in NBCe1 trafficking. We demonstrated that W13 decreases surface expression of NBCe1, accumulates NBCe1-EGFP in endosomal-like formations and inhibits NBCe1 current. W13 and ANGII applied together produces greater inhibition of NBCe1 current than either alone, while W13 and monensin applied together do not. The additive effect of ANGII and W13 and lack of additive effect of monensin and W13 suggest that calmodulin is not involved in ANGII-stimulation of internalization but controls recycling of endocytosed NBCe1. The CaM-activated enzyme CaMKII applied with ANGII also gives an additive inhibitory effect, suggesting a role for CaMKII in NBCe1 recycling.