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J Biol Chem, Vol. 274, Issue 19, 12979-12983, May 7, 1999
From the Department of Biology, Utah State University, Logan, Utah
84322-5305
The SEC14 gene in Saccharomyces
cerevisiae encodes a phosphatidylinositol transfer protein
required for secretory protein movement from the Golgi. Mutation of
SAC1, a gene of unknown function, restores secretory flow
in sec14-1ts strains. The existing model for
the bypass of the sec14-1ts defect by
sac1-22 involves stimulation of sphingolipid biosynthesis and, in particular, the synthesis of
mannosyl-diinositolphosphoryl-ceramide with concomitant increases in
Golgi diacylglycerol levels. To test this model, we disrupted
IPT1, the mannosyl-diinositolphosphoryl-ceramide synthase
of S. cerevisiae. Disruption of the IPT1 gene
had no effect on the ability of sac1-22 to bypass
sec14-1ts. Furthermore, sphingolipid analysis
of sec14-1ts and
sec14-1ts sac1-22 strains showed
that mannosyl-diinositolphosphoryl-ceramide synthesis was not
stimulated in the bypass mutant. However, the sec14-1ts strain had elevated
mannosyl-monoinositolphosphoryl-ceramide levels, and the
sec14-1ts sac1-22 strain showed an
8-fold increase in phosphatidylinositol 4-phosphate along with a
decrease in phosphatidylinositol 4,5-bisphosphate. Cellular
diacylglycerol levels, measured by [14C]acetate
incorporation, did not differ between the
sec14-1ts and the sec14-1 sac1-22
bypass strains, although disruption of IPT1 in the bypass
strain resulted in reduced levels. These data indicate that
phosphatidylinositol 4-phosphate, rather than
mannosyl-diinositolphosphoryl-ceramide, accumulates in the
sec14-1ts sac1-22 bypass strain,
and that Golgi diacylglycerol accumulation is not required for
bypass of the sec14-1ts growth and secretory phenotypes.
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