The polymeric immunoglobulin receptor (pIgR) is transcytosed from the basolateral to the apical surface of polarized epithelial cells. We have previously shown that phosphorylation of Ser-664 in the cytoplasmic domain of the pIgR is a signal for its transcytosis. We now report that binding of a physiological ligand, dimeric IgA, to pIgR stimulates pIgR transcytosis. This stimulation occurs in both the presence or absence of Ser-664 phosphorylation. We have used three methods to measure transcytosis of the pIgR. (i) The pIgR was biosynthetically labeled and its cleavage to secretory component after transcytosis was measured. (ii) The pIgR was labeled with biotin at the basolateral surface. After transcytosis, release of the biotin-labeled secretory component into the apical medium was measured. (iii) Transcytosis of a ligand bound to the pIgR was measured. All three methods indicated that dimeric IgA stimulates transcytosis of the pIgR.