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Vol. 13, Issue 7, 2486-2501, July 2002
Cell Biology and Metabolism Branch, National Institute of Child
Health and Human Development, National Institutes of Health, Bethesda,
Maryland 20892
The biosynthetic sorting of hydrolases to the yeast vacuole
involves transport along two distinct routes referred to as the carboxypeptidase Y and alkaline phosphatase pathways. To identify genes
involved in sorting to the vacuole, we conducted a genome-wide screen
of 4653 homozygous diploid gene deletion strains of
Saccharomyces cerevisiae for missorting of
carboxypeptidase Y. We identified 146 mutant strains that secreted
strong-to-moderate levels of carboxypeptidase Y. Of these, only 53 of
the corresponding genes had been previously implicated in vacuolar
protein sorting, whereas the remaining 93 had either been identified in
screens for other cellular processes or were only known as hypothetical
open reading frames. Among these 93 were genes encoding: 1) the
Ras-like GTP-binding proteins Arl1p and Arl3p, 2) actin-related
proteins such as Arp5p and Arp6p, 3) the monensin and brefeldin A
hypersensitivity proteins Mon1p and Mon2p, and 4) 15 novel proteins
designated Vps61p-Vps75p. Most of the novel gene products were involved
only in the carboxypeptidase Y pathway, whereas a few, including Mon1p,
Mon2p, Vps61p, and Vps67p, appeared to be involved in both the
carboxypeptidase Y and alkaline phosphatase pathways. Mutants lacking
some of the novel gene products, including Arp5p, Arp6p, Vps64p, and
Vps67p, were severely defective in secretion of mature 
-factor.
Others, such as Vps61p, Vps64p, and Vps67p, displayed defects in the
actin cytoskeleton at 30°C. The identification and phenotypic
characterization of these novel mutants provide new insights into the
mechanisms of vacuolar protein sorting, most notably the probable
involvement of the actin cytoskeleton in this process.
Online versions of this article
contain complete data sets.
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