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Vol. 11, Issue 5, 1687-1696, May 2000
and
Departments of *Cell Biology and The tight junction is the most apical intercellular junction of
epithelial cells and regulates transepithelial permeability through the
paracellular pathway. To examine possible functions for the tight
junction-associated protein ZO-1, C-terminally truncated mutants and a
deletion mutant of ZO-1 were epitope tagged and stably expressed in
corneal epithelial cell lines. Only full-length ZO-1 and one N-terminal
truncation mutant targeted to cell borders; other mutants showed
variable cytoplasmic distributions. None of the mutants initially
disrupted the localization of endogenous ZO-1. However, long-term
stable expression of two of the N-terminal mutants resulted in a
dramatic change in cell shape and patterns of gene expression. An
elongated fibroblast-like shape replaced characteristic epithelial
cobblestone morphology. In addition, vimentin and smooth muscle actin
expression were up-regulated, although variable cytokeratin
expression remained, suggesting a partial transformation to a
mesenchymal cell type. Concomitant with the morphological change, the
expression of the integral membrane tight junction protein occludin was
significantly down-regulated. The localizations of endogenous ZO-1 and
another family member, ZO-2, were disrupted. These findings suggest
that ZO-1 may participate in regulation of cellular differentiation.
Neurobiology,
Harvard Medical School, Boston, Massachusetts 02115
Corresponding author. E-mail address:
daniel_goodenough{at}hms.harvard.edu.
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