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Vol. 12, Issue 8, 2257-2274, August 2001
and
*Renal-Electrolyte Division of the Department of Medicine,
Laboratory of Epithelial Biology, and Department of Cell Biology and
Physiology, University of Pittsburgh, Pittsburgh, Pennsylvania 15261;
and Polarized epithelial cells maintain the asymmetric composition of
their apical and basolateral membrane domains by at least two different
processes. These include the regulated trafficking of macromolecules
from the biosynthetic and endocytic pathway to the appropriate membrane
domain and the ability of the tight junction to prevent free mixing of
membrane domain-specific proteins and lipids. Cdc42, a Rho family
GTPase, is known to govern cellular polarity and membrane traffic in
several cell types. We examined whether this protein regulated tight
junction function in Madin-Darby canine kidney cells and pathways that
direct proteins to the apical and basolateral surface of these cells.
We used Madin-Darby canine kidney cells that expressed dominant-active
or dominant-negative mutants of Cdc42 under the control of a
tetracycline-repressible system. Here we report that expression of
dominant-active Cdc42V12 or dominant-negative Cdc42N17 altered tight
junction function. Expression of Cdc42V12 slowed endocytic and
biosynthetic traffic, and expression of Cdc42N17 slowed apical
endocytosis and basolateral to apical transcytosis but stimulated
biosynthetic traffic. These results indicate that Cdc42 may modulate
multiple cellular pathways required for the maintenance of epithelial
cell polarity.
Department of Internal Medicine, National Taiwan
University Hospital, Taipei, 100 Taiwan
Corresponding author. E-mail address:
gla6{at}pitt.edu.
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