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dc.contributor.authorAgre, Peter
dc.contributor.authorGuggino, WB
dc.contributor.authorNielsen, S
dc.contributor.authorKwon, TH
dc.contributor.authorHazama, A.
dc.contributor.authorYasui, M.
dc.date.accessioned2010-05-13T14:35:57Z
dc.date.available2010-05-13T14:35:57Z
dc.date.issued1992-11-11
dc.identifier.citationNature 402, 184-187 (11 November 1999) | doi:10.1038/46045en_US
dc.identifier.urihttp://jhir.library.jhu.edu/handle/1774.2/34111
dc.description.abstractAquaporin (AQP) water-channel proteins are freely permeated by water but not by ions or charged solutes. Although mammalian aquaporins were believed to be located in plasma membranes, rat AQP6 is restricted to intracellular vesicles in renal epithelia. Here we show that AQP6 is functionally distinct from other known aquaporins. When expressed in Xenopus laevis oocytes, AQP6 exhibits low basal water permeability; however, when treated with the known water channel inhibitor, Hg2+, the water permeability of AQP6 oocytes rapidly rises up to tenfold and is accompanied by ion conductance. AQP6 colocalizes with H+-ATPase in intracellular vesicles of acid-secreting alpha-intercalated cells in renal collecting duct. At pH less than 5.5, anion conductance is rapidly and reversibly activated in AQP6 oocytes. Site-directed mutation of lysine to glutamate at position 72 in the cytoplasmic mouth of the pore changes the cation/anion selectivity, but leaves low pH activation intact. Our results demonstrate unusual biophysical properties of an aquaporin, and indicate that anion-channel function may now be explored in a protein with known structure.en_US
dc.language.isoen_USen_US
dc.publisherNature Publishing Groupen_US
dc.subjectIon Channel Gating/drug effectsen_US
dc.subjectAquaporins/metabolismen_US
dc.titleRapid gating and anion permeability of an intracellular aquaporinen_US
dc.typeArticleen_US


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