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(Received for publication, August 15, 1997)
From the Department of Biochemistry and the Lucille P. Markey
Cancer Center, University of Kentucky Medical Center,
Lexington, Kentucky 40536-0084
The ability of organisms to quickly respond to
stresses requires the activation of many intracellular signal
transduction pathways. The sphingolipid intermediate ceramide is
thought to be particularly important for activating and coordinating
signaling pathways during mammalian stress responses. Here we present
the first evidence that ceramide and other sphingolipid intermediates are signaling molecules in the Saccharomyces cerevisiae
heat stress response. Our data show a 2-3-fold transient increase in
the concentration of C18-dihydrosphingosine and
C18-phytosphingosine, more than a 100-fold transient
increase in C20-dihydrosphingosine and
C20-phytosphingosine, and a more stable 2-fold increase in
ceramide containing C18-phytosphingosine and a 5-fold
increase in ceramide containing C20-phytosphingosine following heat stress. Treatment of cells with dihydrosphingosine activates transcription of the TPS2 gene encoding a subunit
of trehalose synthase and causes trehalose, a known thermoprotectant, to accumulate. Dihydrosphingosine induces expression of a
STRE-LacZ reporter gene, showing that the
global stress response element, STRE, found in many yeast
promoter sequences can be activated by sphingolipid signals. The
TPS2 promoter contains four STREs that may
mediate dihydrosphingosine responsiveness. Using genetic and other
approaches it should be possible to identify sphingolipid signaling
pathways in S. cerevisiae and quantify the importance of
each during heat stress.
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