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Vol. 12, Issue 4, 1117-1129, April 2001
*Department of Cell Biology, University of Alabama at Birmingham,
Birmingham, Alabama 35294-0005; and Yeast phosphatidylinositol-transfer protein (Sec14p)
is essential for Golgi secretory function and cell viability. This
requirement of Sec14p is relieved by genetic inactivation of the
cytidine diphosphate-choline pathway for phosphatidycholine (PtdCho)
biosynthesis. Standard phenotypic analyses indicate that inactivation
of the phosphatidylethanolamine (PtdEtn) pathway for PtdCho
biosynthesis, however, does not rescue the growth and secretory defects
associated with Sec14p deficiency. We now report inhibition of choline
uptake from the media reveals an efficient "bypass Sec14p"
phenotype associated with PtdEtn-methylation pathway defects. We
further show that the bypass Sec14p phenotype associated with
PtdEtn-methylation pathway defects resembles other bypass Sec14p
mutations in its dependence on phospholipase D activity. Finally, we
find that increased dosage of enzymes that catalyze phospholipase
D-independent turnover of PtdCho, via mechanisms that do not result in
a direct production of phosphatidic acid or diacylglycerol, effect a
partial rescue of sec14-1ts-associated
growth defects. Taken together, these data support the idea that PtdCho
is intrinsically toxic to yeast Golgi secretory function.
Department of Cell
and Developmental Biology, University of North Carolina at Chapel Hill,
Chapel Hill, North Carolina 27599
Corresponding author. E-mail address:
bktis{at}med.unc.edu.
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