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Vol. 11, Issue 1, 287-304, January 2000
§
*Department of Molecular and Cellular Physiology, Stanford
University School of Medicine, Stanford, California 94305-5345; and
Madin-Darby canine kidney (MDCK) cells expressing constitutively
active Rac1 (Rac1V12) accumulate a large central aggregate of membranes
beneath the apical membrane that contains filamentous actin, Rac1V12,
rab11, and the resident apical membrane protein GP-135. To
examine the roles of Rac1 in membrane traffic and the formation of this
aggregate, we analyzed endocytic and biosynthetic trafficking pathways
in MDCK cells expressing Rac1V12 and dominant inactive Rac1 (Rac1N17).
Rac1V12 expression decreased the rates of apical and basolateral
endocytosis, whereas Rac1N17 expression increased those rates from both
membrane domains. Basolateral-to-apical transcytosis of immunoglobulin
A (IgA) (a ligand for the polymeric immunoglobulin receptor [pIgR]),
apical recycling of pIgR-IgA, and accumulation of newly synthesized
GP-135 at the apical plasma membrane were all decreased in cells
expressing Rac1V12. These effects of Rac1V12 on trafficking pathways to
the apical membrane were the result of the delivery and trapping of
these proteins in the central aggregate. In contrast to abnormalities
in apical trafficking events, basolateral recycling of transferrin,
degradation of EGF internalized from the basolateral membrane, and
delivery of newly synthesized pIgR from the Golgi to the basolateral
membrane were all relatively unaffected by Rac1V12 expression. Rac1N17 expression had little or no effect on these postendocytic or
biosynthetic trafficking pathways. These results show that in polarized
MDCK cells activated Rac1 may regulate the rate of endocytosis from both membrane domains and that expression of dominant active Rac1V12 specifically alters postendocytic and biosynthetic membrane traffic directed to the apical, but not the basolateral, membrane.
Renal-Electrolyte Division of the Department of Medicine
and Laboratory of Epithelial Biology, University of Pittsburgh,
Pittsburgh, Pennsylvania 15261
Present address: 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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