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Am J Physiol Cell Physiol (January 2, 2002). doi:10.1152/ajpcell.00420.2001
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Articles in PresS, published online ahead of print January 2, 2002
Am J Physiol Cell Physiol, 10.1152/ajpcell.00420.2001
Submitted on August 31, 2001
Accepted on December 21, 2001

Human Na+/H+ Exchanger Isoform 6 is Found in the Recycling Endosomes of Cells, Not Mitochondria

Christopher L Brett1, Ying Wei2, Mark Donowitz1, and Rajini Rao2*

1 Physiology, Johns Hopkins University School of Medicine, Baltimore, MD, USA; Medicine, Johns Hopkins University School of Medicine, Baltimore, MD, USA
2 Physiology, Johns Hopkins University School of Medicine, Baltimore, MD, USA

* To whom correspondence should be addressed. E-mail: rrao{at}jhmi.edu.

Since the discovery of the first intracellular Na+/H+ exchanger in yeast, Nhx1, multiple homologues have been cloned and characterized in plants. Together, studies in these organisms demonstrate that Nhx1 is located in the prevacuolar/vacuolar compartment of cells where it sequesters Na+ into the vacuole, regulates intravesicular pH, and contributes to vacuolar biogenesis. In contrast, the human homologue of Nhx1, NHE6, has been reported to localize to mitochondria when transiently expressed as a fusion with green fluorescent protein. This result warrants re-evaluation because it conflicts with predictions from phylogenetic analyses. Here we demonstrate that when epitope-tagged NHE6 is transiently expressed in cultured mammalian cells, it does not colocalize with mitochondrial markers. It also does not colocalize with markers of the lysosome, late endosome, trans-Golgi network, or Golgi cisternae. Rather, NHE6 is distributed in recycling compartments and transiently appears on the plasma membrane. These results suggest that like its homologues in yeast and plants, NHE6 is an endosomal Na+/H+ exchanger that may regulate intravesicular pH and volume, and contribute to lysosomal biogenesis.




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