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Vol. 9, Issue 4, 901-915, April 1998

Dimerization of the Polymeric Immunoglobulin Receptor Controls Its Transcytotic Trafficking

Karen L. Singer,* and Keith E. Mostovdagger

Department of Anatomy and Department of Biochemistry and Biophysics, and Cardiovascular Research Institute, University of California, San Francisco, California 94143-0452

Binding of dimeric immunoglobulin (Ig)A to the polymeric Ig receptor (pIgR) stimulates transcytosis of pIgR across epithelial cells. Through the generation of a series of pIgR chimeric constructs, we have tested the ability of ligand to promote receptor dimerization and the subsequent role of receptor dimerization on its intracellular trafficking. Using the cytoplasmic domain of the T cell receptor-zeta chain as a sensitive indicator of receptor oligomerization, we show that a pIgR:zeta chimeric receptor expressed in Jurkat cells initiates a zeta -specific signal transduction cascade when exposed to dimeric or tetrameric IgA, but not when exposed to monomeric IgA. In addition, we replaced the pIgR's transmembrane domain with that of glycophorin A to force dimerization or with a mutant glycophorin transmembrane domain to prevent dimerization. Forcing dimerization stimulated transcytosis of the chimera, whereas preventing dimerization abolished ligand-stimulated transcytosis. We conclude that binding of dimeric IgA to the pIgR induces its dimerization and that this dimerization is necessary and sufficient to stimulate pIgR transcytosis.

Molecular Biology of the Cell
Vol. 9, 901-915, April 1998
Copyright © 1998 by The American Society for Cell Biology


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