Transcytosis of the polymeric immunoglobulin receptor is regulated in multiple intracellular compartments.

W Song, G Apodaca, K Mostov - Journal of Biological Chemistry, 1994 - Elsevier
Journal of Biological Chemistry, 1994Elsevier
Transcytosis of the polymeric immunoglobulin receptor (pIgR) can be experimentally divided
into three steps: 1) internalization from the basolateral plasma membrane and delivery to
basolateral early endosomes, 2) microtubule-dependent movement from basolateral early
endosomes to apical recycling endosomes, and 3) delivery from apical recycling
endosomes to the apical surface and cleavage of the pIgR to secretory component, which is
released into the apical medium. Transcytosis of the pIgR is stimulated by two signals …
Transcytosis of the polymeric immunoglobulin receptor (pIgR) can be experimentally divided into three steps: 1) internalization from the basolateral plasma membrane and delivery to basolateral early endosomes, 2) microtubule-dependent movement from basolateral early endosomes to apical recycling endosomes, and 3) delivery from apical recycling endosomes to the apical surface and cleavage of the pIgR to secretory component, which is released into the apical medium. Transcytosis of the pIgR is stimulated by two signals, phosphorylation of Ser-664 in the cytoplasmic domain of the pIgR and binding of the ligand, dimeric IgA, to the pIgR. These signals do not detectably alter step 1 of transcytosis. Here, we show that phosphorylation of Ser-664 stimulates both steps 2 and 3, whereas binding of dimeric IgA stimulates only step 3 of transcytosis.
Elsevier