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J. Biol. Chem., Vol. 277, Issue 45, 43495-43504, November 8, 2002
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From the The TOR (target of rapamycin) pathway
controls cell growth in response to nutrient availability in eukaryotic
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 mitogen-activated protein kinase pathway is
regulated by TOR function because upon specific Tor1 and Tor2
inhibition by rapamycin, Mpk1 is activated rapidly in a process
mediated by Sit4 and Tap42. Osmotic stabilization of the plasma
membrane prevents both Mpk1 activation by rapamycin and the growth
defect that occurs upon the simultaneous absence of Tor1 and Mpk1
function, 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
induces 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 pathway, and we provide further evidence demonstrating that Mpk1 is
essential for viability once cells enter G0.
Regulation of the Cell Integrity Pathway by Rapamycin-sensitive
TOR Function in Budding Yeast*
,, and¶
Departament de Ciències Mèdiques
Bàsiques, Universitat de Lleida, Lleida 25198, Spain and the
§ Aureon Biosciences Corporation,
Yonkers, New York 10701
*
This work was supported by Grants 2001 S6R-00305
(Generalitat de Catalunya, Spain) and BMC 2001-1213-C02-01 (Ministerio
de Ciencia y Tecnologia, Spain (MCYT)) (to E. H.), a Generalitat de
Catalunya fellowship (to J. T.), and a Spanish MCYT postdoctoral contract (to M. A. T. R.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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