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J Biol Chem, Vol. 273, Issue 33, 21054-21060, August 14, 1998
From the Department of Physiology, The Johns Hopkins University
School of Medicine, Baltimore, Maryland 21205
Na+/H+ exchangers
catalyze the electrically silent countertransport of Na+
and H+, controlling the transmembrane movement of salt,
water, and acid-base equivalents, and are therefore critical for
Na+ tolerance, cell volume control, and pH regulation. In
contrast to numerous well studied plasma membrane isoforms
(NHE1-4), much less is known about intracellular
Na+/H+ exchangers, and thus far no vertebrate
isoform has been shown to have an exclusively endosomal distribution.
In this context, we show that the yeast NHE homologue, Nhx1 (Nass, R.,
Cunningham, K. W., and Rao, R. (1997) J. Biol. Chem.
272, 26145-26152), localizes uniquely to prevacuolar
compartments, equivalent to late endosomes of animal cells. In living
yeast, we show that these compartments closely abut the vacuolar
membrane in a striking bipolar distribution, suggesting that vacuole
biogenesis occurs at distinct sites. Nhx1 is the founding member of a
newly emergent cluster of exchanger homologues, from yeasts, worms, and
humans that may share a common intracellular localization. By
compartmentalizing Na+, intracellular exchangers play an
important role in halotolerance; furthermore, we hypothesize that salt
and water movement into vesicles may regulate vesicle volume and pH and
thus contribute to vacuole biogenesis.
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