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Vol. 10, Issue 5, 1409-1427, May 1999
Departments of Anatomy and Biochemistry and Cardiovascular Research
Institute, University of California, San Francisco, California
94143-0452
Transcytosis of the polymeric immunoglobulin
receptor (pIgR) is stimulated by binding of its ligand, dimeric IgA
(dIgA). During this process, dIgA binding at the basolateral surface of
the epithelial cell transmits a signal to the apical region of the
cell, which in turn stimulates the transport of dIgA-pIgR complex from
a postmicrotubule compartment to the apical surface. We have previously
reported that the signal of stimulation was controlled by a
protein-tyrosine kinase (PTK) activated upon dIgA binding. We
now show that this signal of stimulation moves across the cell
independently of pIgR movement or microtubules and acts through the
tyrosine kinase activity by releasing Ca++ from
inositol trisphosphate-sensitive intracellular stores.
Surprisingly we have found that a second independent signal is required
to achieve dIgA-stimulated transcytosis of pIgR. This second signal depends on dIgA binding to the pIgR solely at the basolateral surface
and the ability of pIgR to dimerize. This enables pIgR molecules that
have bound dIgA at the basolateral surface to respond to the signal of
stimulation once they reach the postmicrotubule compartment. We propose
that the use of two signals may be a general mechanism by which
signaling receptors maintain specificity along their signaling and
trafficking pathways.
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