RGD Reference Report - Rapid gating and anion permeability of an intracellular aquaporin. - Rat Genome Database

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Rapid gating and anion permeability of an intracellular aquaporin.

Authors: Yasui, M  Hazama, A  Kwon, T H  Nielsen, S  Guggino, W B  Agre, P 
Citation: Yasui M, etal., Nature. 1999 Nov 11;402(6758):184-7. doi: 10.1038/46045.
RGD ID: 408345219
Pubmed: PMID:10647010   (View Abstract at PubMed)
DOI: DOI:10.1038/46045   (Journal Full-text)

Aquaporin (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.



Gene Ontology Annotations    Click to see Annotation Detail View

Molecular Function

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
Aqp6RatpH-gated chloride channel activity enablesIDA PMID:10647010UniProt 
Aqp6Ratwater channel activity enablesIDA PMID:10647010UniProt 

Objects Annotated

Genes (Rattus norvegicus)
Aqp6  (aquaporin 6)


Additional Information