The Journal of Cell Biology, Vol 125, 67-86, Copyright © 1994 by The Rockefeller University Press

ARTICLES

Receptor-mediated transcytosis of IgA in MDCK cells is via apical recycling endosomes

G Apodaca, LA Katz and KE Mostov
Department of Anatomy, University of California, San Francisco 94143.

Classically, the polymeric immunoglobulin receptor and its ligand, IgA, are thought to be sorted from basolateral early endosomes into transcytotic vesicles that directly fuse with the apical plasma membrane. In contrast, we have found that in MDCK cells IgA is delivered from basolateral endosomes to apical endosomes and only then to the apical cell surface. When internalized from the basolateral surface of MDCK cells IgA is found to accumulate under the apical plasma membrane in a compartment that is accessible to two apically added membrane markers: anti-secretory component Fab fragments, and avidin internalized from the biotinylated apical pole of the cell. This accumulation occurs in the presence of apical trypsin, which prevents internalization of the ligand from the apical cell surface. Using a modification of the diaminobenzidine density-shift assay, we estimate that approximately 80% of basolaterally internalized IgA resides in the apical endosomal compartment. In addition, approximately 50% of basolaterally internalized transferrin, a basolateral recycling protein, has access to this apical endosomal compartment and is efficiently recycled back to the basolateral surface. Microtubules are required for the organization of the apical endosomal compartment and it is dispersed in nocodazole-treated cells. Moreover, this compartment is largely inaccessible to fluid-phase markers added to either pole of the cell, and therefore seems analogous to the recycling endosome described in nonpolarized cells. We propose a model in which transcytosis is not a specialized pathway that uses unique transcytotic vesicles, but rather combines portions of pathways used by non- transcytosing molecules.
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• Leung, S.-M., Chen, D., DasGupta, B. R., Whiteheart, S. W., Apodaca, G. (1998). SNAP-23 Requirement for Transferrin Recycling in StreptolysinO-permeabilized Madin-Darby Canine Kidney Cells. J. Biol. Chem. 273: 17732-17741 [Abstract] [Full Text]  
• Calhoun, B. C., Lapierre, L. A., Chew, C. S., Goldenring, J. R. (1998). Rab11a redistributes to apical secretory canaliculus during stimulation of gastric parietal cells. Am. J. Physiol. Cell Physiol. 275: C163-C170 [Abstract] [Full Text]  
• Luton, F., Cardone, M. H., Zhang, M., Mostov, K. E. (1998). Role of Tyrosine Phosphorylation in Ligand-induced Regulation of Transcytosis of the Polymeric Ig Receptor. Mol. Biol. Cell 9: 1787-1802 [Abstract] [Full Text]  
• Low, S. H., Chapin, S. J., Wimmer, C., Whiteheart, S. W., Komuves, L. G., Mostov, K. E., Weimbs, T. (1998). The SNARE Machinery Is Involved in Apical Plasma Membrane Trafficking in MDCK Cells. JCB 141: 1503-1513 [Abstract] [Full Text]  
• Hunziker, W., Peters, P. J. (1998). Rab17 Localizes to Recycling Endosomes and Regulates Receptor-mediated Transcytosis in Epithelial Cells. J. Biol. Chem. 273: 15734-15741 [Abstract] [Full Text]  
• Futter, C.E., Gibson, A., Allchin, E.H., Maxwell, S., Ruddock, L.J., Odorizzi, G., Domingo, D., Trowbridge, I.S., Hopkins, C.R. (1998). In Polarized MDCK Cells Basolateral Vesicles Arise from Clathrin-{gamma}-adaptin-coated Domains on Endosomal Tubules. JCB 141: 611-623 [Abstract] [Full Text]  
• Rice, J. C., Spence, J. S., Megyesi, J., Safirstein, R. L., Goldblum, R. M. (1998). Regulation of the polymeric immunoglobulin receptor by water intake and vasopressin in the rat kidney. Am. J. Physiol. Renal Physiol. 274: F966-F977 [Abstract] [Full Text]  

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