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Articles in PresS, published online ahead of print August 30, 2001
Am J Physiol Renal Physiol, 10.1152/ajprenal.0168.2001
Submitted on May 29, 2001
Accepted on August 21, 2001
1 Cell Physiol, UMC St Radboud, Nijmegen, Netherlands
2 Physiol Biophysics, Univ Arkansas Medical School, Arkansas, AR, USA
3 Brooklyn College, New York, NY, USA
4 Cell Molecular Physiology, Yale University, New Haven, CT, USA
* To whom correspondence should be addressed. E-mail: peterd{at}sci.kun.nl.
Renal regulation of mammalian water homeostasis is mediated by the Aquaporin-1 (AQP1) water channel, expressed in the apical and basolateral membrane of proximal tubules and descending limbs of Henle, and AQP2, which is redistributed from intracellular vesicles to the apical membrane (AM) of collecting duct cells with vasopressin. In transfected MDCK cells, AQP1 and AQP2 are regulated similarly, indicating that routing elements must reside in their primary sequences. Here we studied the role of the AQP2 C-terminus in the apical routing and shuttling of AQP2. An AQP1 chimera composed of AQP1 with an AQP2 tail (AQP1/2-N220) was only located in the AM, independent of forskolin treatment. Forskolin increased the apical expression of AQP1 and AQP1/2-N220 less than two-fold, whereas that of AQP2 increased more than 4-fold, with concomitant changes in osmotic water permeabilities. The dimeric AQP2 tail coupled to alkaline phosphatase (AQP2-Plap) was retained in intracellular vesicles that were different from those of homotetrameric wt-AQP2, whereas the same protein without the AQP2 tail (TMR-Plap) was only expressed in the AM. In conclusion, our study shows that the AQP2 C-tail is necessary (AQP1/2-N220), but not sufficient (AQP2-Plap), for routing to the AM and that other parts of AQP2 are needed for accumulation of AQP2 in intracellular vesicles.
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