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Vol. 12, Issue 12, 4103-4113, December 2001
Department of Genetics, Howard Hughes Medical Institute, Duke
University Medical Center, Durham, North Carolina 27710
Rapamycin binds and inhibits the Tor protein kinases, which
function in a nutrient-sensing signal transduction pathway that has
been conserved from the yeast Saccharomyces cerevisiae
to humans. In yeast cells, the Tor pathway has been implicated in regulating cellular responses to nutrients, including proliferation, translation, transcription, autophagy, and ribosome biogenesis. We
report here that rapamycin inhibits pseudohyphal filamentous differentiation of S. cerevisiae in response to nitrogen
limitation. Overexpression of Tap42, a protein phosphatase regulatory
subunit, restored pseudohyphal growth in cells exposed to rapamycin.
The tap42-11 mutation compromised pseudohyphal
differentiation and rendered it resistant to rapamycin. Cells lacking
the Tap42-regulated protein phosphatase Sit4 exhibited a pseudohyphal
growth defect and were markedly hypersensitive to rapamycin. Mutations
in other Tap42-regulated phosphatases had no effect on pseudohyphal
differentiation. Our findings support a model in which pseudohyphal
differentiation is controlled by a nutrient-sensing pathway involving
the Tor protein kinases and the Tap42-Sit4 protein phosphatase.
Activation of the MAP kinase or cAMP pathways, or mutation of the Sok2
repressor, restored filamentation in rapamycin treated cells,
supporting models in which the Tor pathway acts in parallel with these
known pathways. Filamentous differentiation of diverse fungi was also blocked by rapamycin, demonstrating that the Tor signaling cascade plays a conserved role in regulating filamentous differentiation in
response to nutrients.
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