Regulation of the cell integrity pathway by rapamycin-sensitive TOR function in budding yeast

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2002Suggested citation
Torres Rosell, Jordi;
Di Como, Charles J.;
Herrero Perpiñán, Enrique;
Torre Ruiz, M. A. de la;
.
(2002)
.
Regulation of the cell integrity pathway by rapamycin-sensitive TOR function in budding yeast.
The Journal of Biological Chemistry, 2002, vol. 277, núm 45, p. 43495-43504.
https://doi.org/10.1074/jbc.M205408200.
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Show full item recordAbstract
The TOR (target of rapamycin) pathway controls cell
growth in response to nutrient availability in eukary-
otic cells. Inactivation of TOR function by rapamycin or
nutrient exhaustion is accompanied by triggering
various cellular mechanisms aimed at overcoming the
nutrient stress. Here we report that in Saccharomyces
cerevisiae the protein kinase C (PKC)-mediated mito-
gen-activated protein kinase pathway is regulated by
TOR function because upon specific Tor1 and Tor2 in-
hibition by rapamycin, Mpk1 is activated rapidly in a
process mediated by Sit4 and Tap42. Osmotic stabiliza-
tion of the plasma membrane prevents both Mpk1 acti-
vation by rapamycin and the growth defect that occurs
upon the simultaneous absence of Tor1 and Mpk1 func-
tion, suggesting that, at least partially, TOR inhibition is
sensed by the PKC pathway at the cell envelope. This
process involves activation of cell surface sensors,
Rom2, and downstream elements of the mitogen-
activated protein kinase cascade. Rapamycin also in-
duces depolarization of the actin cytoskeleton through
the TOR proteins, Sit4 and Tap42, in an osmotically
suppressible manner. Finally, we show that entry into
stationary phase, a physiological situation of nutrient
depletion, also leads to the activation of the PKC path-
way, and we provide further evidence demonstrating
that Mpk1 is essential for viability once cells enter G0.
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The Journal of Biological Chemistry, 2002, vol. 277, núm 45, p. 43495-43504European research projects
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