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1 Program in Membrane Biology and Renal Unit, Department of Medicine, Massachusetts General Hospital and Harvard Medical School, Boston, MA, USA
* To whom correspondence should be addressed. E-mail: brown{at}receptor.mgh.harvard.edu.
Inhibition of clathrin-mediated endocytosis by expression of a GTPase-deficient dynamin mutant (dynamin-2/K44A) for 16 h results in an accumulation of plasma membrane AQP2 in epithelial cells stably transfected with wild type AQP2. We now show a similar effect of K44A dynamin in LLC-PK1 cells transfected with an S256-phosphorylation deficient AQP2 mutant, AQP2(S256A), and in AQP2-transfected IMCD
cells. More acute blockade of endocytosis in these cells with the cholesterol-depleting agent, methyl-beta- cyclodextrin (m
CD - 10 mM) resulted in a rapid and extensive cell surface accumulation of both wild-type AQP2 and AQP2(S256A) within 15 min after treatment. This effect was similar to that induced by treatment of the cells with
vasopressin. Blockade of endocytosis by mCD was confirmed using quantitative analysis of FITC-dextran uptake and AQP2 membrane insertion was verified by cellsurface biotinylation. These data indicate that AQP2 recycles constitutively and rapidly between intracellular stores and the cell surface in LLC-PK1 and IMCD cells. The constitutive trafficking process is not dependent on phosphorylation of the serine 256 residue of AQP2 which is, however, an essential step for regulated, vasopressin/cAMPmediated translocation of AQP2. Our data show that rapid and extensive plasma membrane accumulation of AQP2 can occur in a vasopressin-receptor (V2R)- and
phosphorylation- independent manner, pointing to a potential means of bypassing the mutated V2R in X-linked nephrogenic diabetes insipidus to achieve cell surface
expression of AQP2.
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