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J. Biol. Chem., Vol. 277, Issue 26, 23755-23763, June 28, 2002
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§,,,, and
From the A problem for inositol signaling is to understand
the significance of the kinases that convert inositol hexakisphosphate
to diphosphoinositol polyphosphates. This kinase activity is catalyzed by Kcs1p in the yeast Saccharomyces cerevisiae. A
kcs1 Institut de Recherches Microbiologiques
Jean-Marie Wiame, Université Libre de Bruxelles, Brussels,
Belgium B-1070 and the ¶ Inositide Signaling Section,
Laboratory of Signal Transduction, NIEHS, National Institutes of
Health, Research Triangle Park, North Carolina 27709
yeast strain that was transformed with a
specifically "kinase-dead" kcs1p mutant did not synthesize
diphosphoinositol polyphosphates, and the cells contained a fragmented
vacuolar compartment. Biogenesis of the yeast vacuole also required
another functional domain in Kcs1p, which contains two leucine heptad
repeats. The kinase activity of Kcs1p was also found to sustain cell
growth and integrity of the cell wall and to promote adaptive responses
to salt stress. Thus, the synthesis of diphosphoinositol polyphosphates
has wide ranging physiological significance. Furthermore, we showed
that these phenotypic responses to Kcs1p deletion also arise when
synthesis of precursor material for the diphosphoinositol
polyphosphates is blocked in arg82 cells. This metabolic
block was partially bypassed, and the phenotype was partially rescued,
when Kcs1p was overexpressed in the arg82 cells. This
was due, in part, to the ability of Kcs1p to phosphorylate a wider
range of substrates than previously appreciated. Our results show that
diphosphoinositol polyphosphate synthase activity is essential for
biogenesis of the yeast vacuole and the cell's responses to certain
environmental stresses.
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