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Vol. 10, Issue 4, 1147-1161, April 1999
Vienna Biocenter, Institute of Biochemistry and Molecular Cell
Biology, University of Vienna and Ludwig Boltzmann-Forschungstelle
für Biochemie, A-1030 Vienna, Austria
Budding yeast adjusts to increases in external osmolarity via a
specific mitogen-activated protein kinase signal pathway, the
high-osmolarity glycerol response (HOG) pathway. Studies with a
functional Hog1-green fluorescent protein (GFP) fusion reveal that
even under nonstress conditions the mitogen-activated protein kinase Hog1 cycles between cytoplasmic and nuclear compartments. The
basal distribution of the protein seems independent of its activator,
Pbs2, and independent of its phosphorylation status. Upon osmotic
challenge, the Hog1-GFP fusion becomes rapidly concentrated in the
nucleus from which it is reexported after return to an iso-osmotic
environment or after adaptation to high osmolarity. The preconditions
and kinetics of increased nuclear localization correlate with those
found for the dual phosphorylation of Hog1-GFP. The duration of Hog1
nuclear residence is modulated by the presence of the general stress
activators Msn2 and Msn4. Reexport of Hog1 to the cytoplasm does not
require de novo protein synthesis but depends on Hog1 kinase activity.
Thus, at least three different mechanisms contribute to the
intracellular distribution pattern of Hog1: phosphorylation-dependent
nuclear accumulation, retention by nuclear targets, and a
kinase-induced export.
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