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Vol. 11, Issue 12, 4277-4294, December 2000
Institute of Molecular Biology, University of Oregon, Eugene,
Oregon 97403-1229
We show that the vacuolar protein sorting gene VPS44
is identical to NHX1, a gene that encodes a
sodium/proton exchanger. The Saccharomyces cerevisiae
protein Nhx1p shows high homology to mammalian sodium/proton exchangers
of the NHE family. Nhx1p is thought to transport sodium ions into the
prevacuole compartment in exchange for protons. Pulse-chase
experiments show that ~35% of the newly synthesized soluble vacuolar
protein carboxypeptidase Y is missorted in nhx1
cells, and is secreted from the cell. nhx1 cells accumulate late Golgi, prevacuole, and
lysosome markers in an aberrant structure next to the vacuole, and late
Golgi proteins are proteolytically cleaved more rapidly than in
wild-type cells. Our results show that efficient transport out of the
prevacuolar compartment requires Nhx1p, and that nhx1
cells exhibit phenotypes characteristic of the "class E" group of
vps mutants. In addition, we show that Nhx1p is required
for protein trafficking even in the absence of the vacuolar ATPase. Our
analysis of Nhx1p provides the first evidence that a sodium/proton
exchange protein is important for correct protein sorting, and that
intraorganellar ion balance may be important for endosomal function in yeast.
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