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News Physiol Sci 17: 68-72, 2002;
1548-9213/02 $5.00
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News in Physiological Sciences, Vol. 17, No. 2, 68-72, April 2002
© 2002 Int. Union Physiol. Sci./Am. Physiol. Soc.

New Roles for Old Holes: Ion Channel Function in Aquaporin-1

Andrea J. Yool1 and Alan M. Weinstein2

1 Department of Physiology, Department of Pharmacology, University of Arizona College of Medicine, Tucson Arizona 85724-5051;
2 Department of Physiology, Weill Medical College of Cornell University, New York, New York 10021-4896

Mammalian aquaporins are part of the diverse major intrinsic protein family of water and solute channels. Intriguing links exist in structural and functional properties between aquaporins and ion channels. A novel role for aquaporin-1 as a gated ion channel reshapes our current views of this ancient family of transmembrane channel proteins.




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