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Vol. 11, Issue 8, 2673-2689, August 2000
Division of Cellular and Molecular Medicine, The Howard Hughes
Medical Institute, University of California, San Diego, School of
Medicine, La Jolla, California 92093-0668
The yeast Saccharomyces cerevisiae possesses two
genes that encode phosphatidylinositol (PtdIns) 4-kinases,
STT4 and PIK1. Both gene products
phosphorylate PtdIns at the D-4 position of the inositol ring
to generate PtdIns(4)P, which plays an essential role in yeast
viability because deletion of either STT4 or
PIK1 is lethal. Furthermore, although both enzymes have
the same biochemical activity, increased expression of either kinase
cannot compensate for the loss of the other, suggesting that these
kinases regulate distinct intracellular functions, each of which is
required for yeast cell growth. By the construction of
temperature-conditional single and double mutants, we have found that
Stt4p activity is required for the maintenance of vacuole morphology,
cell wall integrity, and actin cytoskeleton organization. In contrast,
Pik1p is essential for normal secretion, Golgi and vacuole membrane dynamics, and endocytosis. Strikingly,
pik1ts cells exhibit a rapid defect in
secretion of Golgi-modified secretory pathway cargos, Hsp150p and
invertase, whereas stt4ts cells exhibit no
detectable secretory defects. Both single mutants reduce PtdIns(4)P by
~50%; however,
stt4ts/pik1ts
double mutant cells produce more than 10-fold less PtdIns(4)P as
well as PtdIns(4,5)P2. The aberrant Golgi morphology found in pik1ts mutants is strikingly similar to
that found in cells lacking the function of Arf1p, a small GTPase that
is known to regulate multiple membrane trafficking events throughout
the cell. Consistent with this observation, arf1 mutants
exhibit reduced PtdIns(4)P levels. In contrast, diminished levels of
PtdIns(4)P observed in stt4ts cells at
restrictive temperature result in a dramatic change in vacuole size
compared with pik1ts cells and persistent
actin delocalization. Based on these results, we propose that Stt4p and
Pik1p act as the major, if not the only, PtdIns 4-kinases in yeast and
produce distinct pools of PtdIns(4)P and PtdIns(4,5)P2 that
act on different intracellular membranes to recruit or activate as yet
uncharacterized effector proteins.
Corresponding author. E-mail address:
semr{at}ucsd.edu.
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