|
|
||||||||
MEMBRANE TRANSPORTERS, ION CHANNELS, AND PUMPS
1Department of Biological Sciences and 2Renal-Electrolyte Division, Department of Medicine, University of Pittsburgh, Pittsburgh, Pennsylvania; and 3IBLS Division of Molecular Genetics, University of Glasgow, Glasgow, United Kingdom
Submitted 16 December 2004 ; accepted in final form 25 March 2005
Aquaporins (AQPs) accelerate the movement of water and other solutes across biological membranes, yet the molecular mechanisms of each AQP's transport function and the diverse physiological roles played by AQP family members are still being defined. We therefore have characterized an AQP in a model organism, Drosophila melanogaster, which is amenable to genetic manipulation and developmental analysis. To study the mechanism of Drosophila Malpighian tubule (MT)-facilitated water transport, we identified seven putative AQPs in the Drosophila genome and found that one of these, previously named DRIP, has the greatest sequence similarity to those vertebrate AQPs that exhibit the highest rates of water transport. In situ mRNA analyses showed that DRIP is expressed in both embryonic and adult MTs, as well as in other tissues in which fluid transport is essential. In addition, the pattern of DRIP expression was dynamic. To define DRIP-mediated water transport, the protein was expressed in Xenopus oocytes and in yeast secretory vesicles, and we found that significantly elevated rates of water transport correlated with DRIP expression. Moreover, the activation energy required for water transport in DRIP-expressing secretory vesicles was 4.9 kcal/mol. This low value is characteristic of AQP-mediated water transport, whereas the value in control vesicles was 16.4 kcal/mol. In contrast, glycerol, urea, ammonia, and proton transport were unaffected by DRIP expression, suggesting that DRIP is a highly selective water-specific channel. This result is consistent with the homology between DRIP and mammalian water-specific AQPs. Together, these data establish Drosophila as a new model system with which to investigate AQP function.
fluid homeostasis; osmosis; channel; membrane
This article has been cited by other articles:
![]() |
J. P. Day, S. Wan, A. K. Allan, L. Kean, S. A. Davies, J. V. Gray, and J. A. T. Dow Identification of two partners from the bacterial Kef exchanger family for the apical plasma membrane V-ATPase of Metazoa J. Cell Sci., August 1, 2008; 121(15): 2612 - 2619. [Abstract] [Full Text] [PDF] |
||||
![]() |
C. G. Huang, T. Lamitina, P. Agre, and K. Strange Functional analysis of the aquaporin gene family in Caenorhabditis elegans Am J Physiol Cell Physiol, May 1, 2007; 292(5): C1867 - C1873. [Abstract] [Full Text] [PDF] |
||||
![]() |
S. L. Zimmerman, J. Frisbie, D. L. Goldstein, J. West, K. Rivera, and C. M. Krane Excretion and conservation of glycerol, and expression of aquaporins and glyceroporins, during cold acclimation in Cope's gray tree frog Hyla chrysoscelis Am J Physiol Regulatory Integrative Comp Physiol, January 1, 2007; 292(1): R544 - R555. [Abstract] [Full Text] [PDF] |
||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| Visit Other APS Journals Online |