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Vol. 12, Issue 6, 1835-1841, June 2001
Pathology Department and Cell Biology Program, Case Western Reserve
University School of Medicine, Cleveland, Ohio 44106
Hypertonic shock of Saccharomyces cerevisiae
activates the Hog1p MAP kinase cascade. In contrast, protein kinase C
(Pkc1p) and the "cell integrity" MAP kinase cascade are critical
for the response to hypotonic shock. We observed that hypertonic shock transiently relocated many, but not all, nuclear and nucleolar proteins
to the cytoplasm. We hypothesized that the relocation of nuclear
proteins was due to activation of the Hog1p kinase cascade, yet,
surprisingly, Hog1p was not required for these effects. In contrast,
Pkc1p kinase activity was required, although the Pkc1p MAP kinase
cascade and several factors known to lie upstream and downstream of
Pkc1p were not. Moreover, sudden induction of a hyperactive form of
Pkc1p was sufficient to relocate nuclear proteins. Taken together,
these observations show that the scope of involvement of Pkc1p in the
organization of the nucleus considerably exceeds what has been
characterized previously. The relocation of nuclear proteins is likely
to account for the profound inhibition of RNA synthesis that was
observed during hypertonic shock.
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