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1 Università di Bari, Dipartimento di Fisiologia Generale e Ambientale, 70126 Bari, Italy; 2 Forschungsinstitut für Molekulare Pharmakologie, Campus Berlin-Buch, 13125 Berlin; 3 Institut für Pharmakologie und Toxikologie, Albert-Ludwigs-Universität Freiburg, 79104 Freiburg; and 4 Institut für Pharmakologie, Freie Universität Berlin, 14195 Berlin, Germany
First published August 8, 2001;
10.1152/ajprenal.00091.2001.
We have recently demonstrated that actin
depolymerization is a prerequisite for cAMP-dependent translocation of
the water channel aquaporin-2 (AQP2) into the apical membrane in
AQP2-transfected renal CD8 cells (29). The Rho family of
small GTPases, including Cdc42, Rac, and Rho, regulates the actin
cytoskeleton. In AQP2-transfected CD8 cells, inhibition of Rho GTPases
with Clostridium difficile toxin B or with C. limosum C3 fusion toxin, as well as incubation with the Rho kinase
inhibitor, Y-27632, caused actin depolymerization and translocation of
AQP2 in the absence of the cAMP-elevating agent forskolin. Both
forskolin and C3 fusion toxin-induced AQP2 translocation were
associated with a similar increase in the osmotic water permeability
coefficient. Expression of constitutively active RhoA induced formation
of stress fibers and abolished AQP2 translocation in response to
forskolin. Cytochalasin D induced both depolymerization of F-actin and
AQP2 translocation, suggesting that depolymerization of F-actin is
sufficient to induce AQP2 translocation. Together, these data indicate
that Rho inhibits cAMP-dependent translocation of AQP2 into the apical
membrane of renal principal cells by controlling the organization of
the actin cytoskeleton.
aquaporin; C3 toxin; toxin B; actin cytoskeleton; G proteins; adenosine 3',5'-cyclic monophosphate
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