Yeast Genetics and Molecular Biology 2000
University of Washington
Seattle, Washington USA
July 2000


Name: Bowers, Katherine
Mailing Address: Institute of Molecular Biology, University of Oregon, 1370 Franklin Blvd, Eugene, OR 97403-1229, USA
Email Address: kbowers@molbio.uoregon.edu
Phone & FAX numbers: 011-541-436-4608 & 011-541-346-4854

#016

A prevacuolar sodium/proton exchanger, Nhx1p, is required for vacuolar protein sorting in Saccharomyces cerevisiae.
Katherine Bowers, Boaz P. Levi, Falguny I. Patel, Tom H. Stevens
Institute of Molecular Biology, University of Oregon, 1370 Franklin Blvd, Eugene, OR 97403-1229, USA

Genetic screens in yeast have identified over 50 vacuolar protein sorting (vps)genes, involved in membrane trafficking from the late Golgi to the vacuole. We show that VPS44is 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. We have cloned the NHX1gene and introduced a C-terminal triple HA tag. We have also deleted NHX1in a haploid yeast strain (nhx1delta). Pulse-chase experiments show that approximately 35% of the newly synthesized soluble vacuolar protein carboxypeptidase Y is missorted in the nhx1delta cells, and is secreted from the cell. nhx1delta 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 nhx1delta cells exhibit phenotypes characteristic of the 'class E' group of vpsmutants. 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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