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Vol. 9, Issue 7, 1787-1802, July 1998
Departments of Anatomy and Biochemistry, and Cardiovascular
Research Institute, University of California, San Francisco,
California 94143-0452
The polymeric Ig receptor (pIgR) transcytoses its ligand, dimeric
IgA (dIgA), from the basolateral to the apical surface of epithelial
cells. Although the pIgR is constitutively transcytosed in the absence
of ligand, binding of dIgA stimulates transcytosis of the pIgR. We
recently reported that dIgA binding to the pIgR induces translocation
of protein kinase C, production of inositol triphosphate, and
elevation of intracellular free calcium. We now report that dIgA
binding causes rapid, transient tyrosine phosphorylation of several
proteins, including phosphatidyl inositol-specific phospholipase C-
l. Protein tyrosine kinase inhibitors or deletion of
the last 30 amino acids of pIgR cytoplasmic tail prevents
IgA-stimulated protein tyrosine kinase activation, tyrosine
phosphorylation of phospholipase C-l, production of inositol
triphosphate, and the stimulation of transcytosis by dIgA. Analysis of
pIgR deletion mutants reveals that the same discrete portion of the
cytoplasmic domain, residues 727-736 (but not the Tyr734), controls
both the ability of pIgR to cause dIgA-induced tyrosine phosphorylation of the phospholipase C-l and to undergo dIgA-stimulated
transcytosis. In addition, dIgA transcytosis can be strongly stimulated
by mimicking phospholipase C-l activation. In combination with our
previous results, we conclude that the protein tyrosine kinase(s) and
phospholipase C-l that are activated upon dIgA binding to the pIgR
control dIgA-stimulated pIgR transcytosis.
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