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Vol. 10, Issue 7, 2235-2250, July 1999
and
Departments of *Cell Biology and §Pathology,
University of Alabama at Birmingham, Birmingham, Alabama 35294-0005;
SacIp dysfunction results in bypass of the
requirement for phosphatidylinositol transfer protein (Sec14p)
function in yeast Golgi processes. This effect is accompanied by
alterations in inositol phospholipid metabolism and
inositol auxotrophy. Elucidation of how sac1
mutants effect "bypass Sec14p" will provide insights into
Sec14p function in vivo. We now report that, in addition to a dramatic
accumulation of phosphatidylinositol-4-phosphate, sac1 mutants also exhibit a specific acceleration of
phosphatidylcholine biosynthesis via the CDP-choline pathway.
This phosphatidylcholine metabolic phenotype is sensitive to the two
physiological challenges that abolish bypass Sec14p in
sac1 strains; i.e. phospholipase D inactivation and
expression of bacterial diacylglycerol (DAG) kinase. Moreover, we
demonstrate that accumulation of
phosphatidylinositol-4-phosphate in sac1
mutants is insufficient to effect bypass Sec14p. These data support a
model in which phospholipase D activity contributes to generation of
DAG that, in turn, effects bypass Sec14p. A significant fate for this
DAG is consumption by the CDP-choline pathway. Finally, we determine
that CDP-choline pathway activity contributes to the inositol
auxotrophy of sac1 strains in a novel manner that does
not involve obvious defects in transcriptional expression of the
INO1 gene.
Department of Pharmacology and Cancer Biology, Duke
University Medical Center, Durham, North Carolina 27710;
Department of Basic Allied Medicine, Gunma University
School of Health Sciences, Maebashi 371, Japan; and
¶Department of Biological Science, Nara Women's
University, Nara 630-8506, Japan
These authors contributed equally to this work.
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