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A more recent version of this article appeared on January 1, 2004
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Submitted on May 20, 2003
Revised on August 26, 2003
Accepted on September 4, 2003
1 Epithelial Pathobiology Research Unit, Department of Pathology and Laboratory Medicine, Emory University, Atlanta, Georgia 30322
* Corresponding author. E-mail address: aiivano{at}emory.edu.
The adherens junction (AJ*) and tight junction (TJ) are key
regulators of epithelial polarity and barrier function. Loss of
epithelial phenotype is accompanied by endocytosis of AJs and TJs via
unknown mechanisms. Using a model of calcium depletion, we defined the
pathway of internalization of AJ and TJ proteins (E-cadherin, p120 and
-catenins, occludin, JAM-1, claudins 1 and 4, and ZO-1) in T84
epithelial cells. Proteinase protection assay and immunocytochemistry
revealed orchestrated internalization of AJs and TJs into a subapical
cytoplasmic compartment. Disruption of caveolae/lipid rafts did not
prevent endocytosis, nor did caveolin-1 colocalize with internalized
junctional proteins. Furthermore, AJ and TJ proteins did not colocalize
with the macropinocytosis marker dextran. Inhibitors of
clathrin-mediated endocytosis blocked internalization of AJs and TJs,
and junctional proteins colocalized with clathrin and 
-adaptin. AJ
and TJ proteins were observed to enter early endosomes followed by
movement to organelles that stained with syntaxin-4 but not with
markers of late and recycling endosomes, lysosomes or Golgi. These
results indicate that endocytosis of junctional proteins is a
clathrin-mediated process leading into a unique storage compartment.
Such mechanisms may mediate the disruption of intercellular contacts
during normal tissue remodeling and in pathology.
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