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Vol. 10, Issue 12, 4263-4281, December 1999
Division of Biological Sciences, University of Missouri,
Columbia, Missouri 65211
The proper localization of resident membrane proteins to the
trans-Golgi network (TGN) involves mechanisms for both
TGN retention and retrieval from post-TGN compartments. In this study
we report identification of a new gene, GRD20, involved
in protein sorting in the TGN/endosomal system of Saccharomyces
cerevisiae. A strain carrying a transposon insertion allele of
GRD20 exhibited rapid vacuolar degradation of the
resident TGN endoprotease Kex2p and aberrantly secreted ~50% of the
soluble vacuolar hydrolase carboxypeptidase Y. The Kex2p
mislocalization and carboxypeptidase Y missorting phenotypes
were exhibited rapidly after loss of Grd20p function in
grd20 temperature-sensitive mutant strains, indicating
that Grd20p plays a direct role in these processes. Surprisingly,
little if any vacuolar degradation was observed for the TGN membrane proteins A-ALP and Vps10p, underscoring a difference in trafficking patterns for these proteins compared with that of Kex2p. A
grd20 null mutant strain exhibited extremely slow growth
and a defect in polarization of the actin cytoskeleton, and these two
phenotypes were invariably linked in a collection of randomly
mutagenized grd20 alleles. GRD20 encodes
a hydrophilic protein that partially associates with the TGN. The
discovery of GRD20 suggests a link between the
cytoskeleton and function of the yeast TGN.
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