TY - JOUR
T1 - Target of rapamycin in yeast, TOR2, is an essential phosphatidylinositol kinase homolog required for G1 progression
AU - Kunz, Jeannette
AU - Henriquez, Ruben
AU - Schneider, Ulrich
AU - Deuter-Reinhard, Maja
AU - Movva, N. Rao
AU - Hall, Michael N.
N1 - Funding Information:
We thank Jose Garcia-Bustos and Bernard Dujon for the physical mapping of TOR2, Scott Emr for valuable discussions and unpublished data, and the members of the laboratory for comments on the manuscript. The research was supported by a grant from the Swiss National Science Foundation awarded to M. N. H.
Copyright:
Copyright 2015 Elsevier B.V., All rights reserved.
PY - 1993/5/7
Y1 - 1993/5/7
N2 - The yeast TOR2 gene encodes an essential 282 kd phosphatidylinositol (PI) 3-kinase homolog. TOR2 is related to the catalytic subunit of bovine PI 3-kinase and to yeast VPS34, a vacuolar sorting protein also shown to have PI 3-kinase activity. The immunosuppressant rapamycin most likely acts by inhibiting PI kinase activity because TOR2 mutations confer resistance to rapamycin and because a TOR1 TOR2 double disruption (TOR1 is a nonessential TOR2 homolog) confers G1 arrest, as does rapamycin. Our results further suggest that 3-phosphorylated phosphoinositides, whose physiological significance has not been determined, are an important signal in cell cycle activation. In yeast, this signal may act in a signal transduction pathway similar to the interleukin-2 signal transduction pathway in T cells.
AB - The yeast TOR2 gene encodes an essential 282 kd phosphatidylinositol (PI) 3-kinase homolog. TOR2 is related to the catalytic subunit of bovine PI 3-kinase and to yeast VPS34, a vacuolar sorting protein also shown to have PI 3-kinase activity. The immunosuppressant rapamycin most likely acts by inhibiting PI kinase activity because TOR2 mutations confer resistance to rapamycin and because a TOR1 TOR2 double disruption (TOR1 is a nonessential TOR2 homolog) confers G1 arrest, as does rapamycin. Our results further suggest that 3-phosphorylated phosphoinositides, whose physiological significance has not been determined, are an important signal in cell cycle activation. In yeast, this signal may act in a signal transduction pathway similar to the interleukin-2 signal transduction pathway in T cells.
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U2 - 10.1016/0092-8674(93)90144-F
DO - 10.1016/0092-8674(93)90144-F
M3 - Article
C2 - 8387896
AN - SCOPUS:0027311858
VL - 73
SP - 585
EP - 596
JO - Cell
JF - Cell
SN - 0092-8674
IS - 3
ER -