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Vol. 10, Issue 12, 4369-4384, December 1999
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 Efficient postendocytic membrane traffic in polarized epithelial
cells is thought to be regulated in part by the actin
cytoskeleton. RhoA modulates assemblies of actin in the cell,
and it has been shown to regulate pinocytosis and phagocytosis;
however, its effects on postendocytic traffic are largely unexplored.
To this end, we expressed wild-type RhoA (RhoAWT), dominant active RhoA
(RhoAV14), and dominant inactive RhoA (RhoAN19) in Madin-Darby canine
kidney (MDCK) cells expressing the polymeric immunoglobulin receptor. RhoAV14 expression stimulated the rate of apical and basolateral endocytosis, whereas RhoAN19 expression decreased the rate from both
membrane domains. Polarized basolateral recycling of transferrin was
disrupted in RhoAV14-expressing cells as a result of increased ligand
release at the apical pole of the cell. Degradation of basolaterally
internalized epidermal growth factor was slowed in RhoAV14-expressing
cells. Although apical recycling of immunoglobulin A (IgA) was largely
unaffected in cells expressing RhoAV14, transcytosis of basolaterally
internalized IgA was severely impaired. Morphological and biochemical
analyses demonstrated that a large proportion of IgA internalized from
the basolateral pole of RhoAV14-expressing cells remained within
basolateral early endosomes and was slow to exit these compartments.
RhoAN19 and RhoAWT expression had little effect on these postendocytic
pathways. These results indicate that in polarized MDCK cells activated
RhoA may modulate endocytosis from both membrane domains and
postendocytic traffic at the basolateral pole of the cell.
Graduate Institute of Clinical
Medicine, College of Medicine, National Taiwan University, Taipei, 100 Taiwan
Corresponding author. E-mail address:
gla6{at}pitt.edu.
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