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Center for Research and Advanced Studies, 07000 Mexico City, Mexico
The tight junction (TJ) was first noticed through its ability to
control permeation across the paracellular route, but the homologies of
its molecular components with peptides that participate in tumor
suppression, nuclear addressing, and cell proliferation indicate that
it may be involved in many other fundamental functions. TJs are formed
by a dozen molecular species that assemble through PDZ and other
protein-protein clustering promoting sequences, in response to the
activation of E-cadherin. The TJ occupies a highly specific position
between the apical and the basolateral domains. Its first molecular
components seem to be delivered to such a position by addressing
signals in their molecule and, once anchored, serve as a clustering
nucleus for further TJ-associated molecules. Although in mature
epithelial cells TJs and E-cadherin do not colocalize, a complex chain
of reactions goes from one to the other that involves
-,
-, and
-catenins, two different G proteins, phospholipase C, protein kinase
C, calmodulin, mitogen-activated protein kinase, and molecules
pertaining to the cytoskeleton, which keep the TJ sensitive to
physiological requirements and local conditions (notably to
Ca2+-dependent cell-cell contacts) throughout the life of
the epithelium.
apical membrane; basolateral membrane; polarity; E-cadherin; zonula occludens-1; occludin
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