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Sci. STKE, 9 December 2003
Vol. 2003, Issue 212, p. re15
[DOI: 10.1126/stke.2122003re15]
REVIEWS
TOR Signaling
Thurl E. Harris and
John C. Lawrence Jr.*
Department of Pharmacology, University of Virginia School of Medicine, Charlottesville, VA 22908, USA.
Abstract:
The mammalian target of rapamycin, mTOR, is a protein Ser-Thr kinase that functions as a central element in a signaling pathway involved in the control of cell growth and proliferation. The activity of mTOR is controlled not only by amino acids, but also by hormones and growth factors that activate the protein kinase Akt. The signaling pathway downstream of Akt leading to mTOR involves the protein products of the genes mutated in tuberous sclerosis, TSC1 and TSC2, and the small guanosine triphosphatase, Rheb. In cells, mTOR is found in a complex with two other proteins, raptor and mLST8. In this review, we describe recent progress in understanding the control of the mTOR signaling pathway and the role of mTOR-interacting proteins.
Mammalian Target of Rapamycin Repression by 3,3'-Diindolylmethane Inhibits Invasion and Angiogenesis in Platelet-Derived Growth Factor-D-Overexpressing PC3 Cells.
D. Kong, S. Banerjee, W. Huang, Y. Li, Z. Wang, H.-R. C. Kim, and F. H. Sarkar (2008)
Cancer Res.
68, 1927-1934
|Abstract »|Full Text »|PDF »
Identifying Breast Cancer Druggable Oncogenic Alterations: Lessons Learned and Future Targeted Options.
Up-regulation of Acetyl-CoA Carboxylase {alpha} and Fatty Acid Synthase by Human Epidermal Growth Factor Receptor 2 at the Translational Level in Breast Cancer Cells.
S. Yoon, M.-Y. Lee, S. W. Park, J.-S. Moon, Y.-K. Koh, Y.-H. Ahn, B.-W. Park, and K.-S. Kim (2007)
J. Biol. Chem.
282, 26122-26131
|Abstract »|Full Text »|PDF »
A Role for Mammalian Target of Rapamycin in Regulating T Cell Activation versus Anergy.
Y. Zheng, S. L. Collins, M. A. Lutz, A. N. Allen, T. P. Kole, P. E. Zarek, and J. D. Powell (2007)
J. Immunol.
178, 2163-2170
|Abstract »|Full Text »|PDF »
Rapamycin inhibits the growth and muscle-sparing effects of clenbuterol.
W. O. Kline, F. J. Panaro, H. Yang, and S. C. Bodine (2007)
J Appl Physiol
102, 740-747
|Abstract »|Full Text »|PDF »
Folliculin encoded by the BHD gene interacts with a binding protein, FNIP1, and AMPK, and is involved in AMPK and mTOR signaling.
M. Baba, S.-B. Hong, N. Sharma, M. B. Warren, M. L. Nickerson, A. Iwamatsu, D. Esposito, W. K. Gillette, R. F. Hopkins III, J. L. Hartley, et al. (2006)
PNAS
103, 15552-15557
|Abstract »|Full Text »|PDF »
Activation of Mammalian Target of Rapamycin (mTOR) by Insulin Is Associated with Stimulation of 4EBP1 Binding to Dimeric mTOR Complex 1.
L. Wang, C. J. Rhodes, and J. C. Lawrence Jr. (2006)
J. Biol. Chem.
281, 24293-24303
|Abstract »|Full Text »|PDF »
Role of Insulin, Adipocyte Hormones, and Nutrient-Sensing Pathways in Regulating Fuel Metabolism and Energy Homeostasis: A Nutritional Perspective of Diabetes, Obesity, and Cancer.
The role of phospholipase D and phosphatidic acid in the mechanical activation of mTOR signaling in skeletal muscle.
T. A. Hornberger, W. K. Chu, Y. W. Mak, J. W. Hsiung, S. A. Huang, and S. Chien (2006)
PNAS
103, 4741-4746
|Abstract »|Full Text »|PDF »
Suppression of the mTOR-Raptor Signaling Pathway by the Inhibitor of Heat Shock Protein 90 Geldanamycin.
G. Ohji, S. Hidayat, A. Nakashima, C. Tokunaga, N. Oshiro, K.-i. Yoshino, K. Yokono, U. Kikkawa, and K. Yonezawa (2006)
J. Biochem.
139, 129-135
|Abstract »|Full Text »|PDF »
Tor2 Directly Phosphorylates the AGC Kinase Ypk2 To Regulate Actin Polarization.
Y. Kamada, Y. Fujioka, N. N. Suzuki, F. Inagaki, S. Wullschleger, R. Loewith, M. N. Hall, and Y. Ohsumi (2005)
Mol. Cell. Biol.
25, 7239-7248
|Abstract »|Full Text »|PDF »
The coordinate regulation of the p53 and mTOR pathways in cells.
Farnesyltransferase inhibitors reverse altered growth and distribution of actin filaments in Tsc-deficient cells via inhibition of both rapamycin-sensitive and -insensitive pathways.
C.-L. Gau, J. Kato-Stankiewicz, C. Jiang, S. Miyamoto, L. Guo, and F. Tamanoi (2005)
Mol. Cancer Ther.
4, 918-926
|Abstract »|Full Text »|PDF »
Post-Transcriptional Regulation of the Androgen Receptor by Mammalian Target of Rapamycin.
B. Cinar, A. De Benedetti, and M. R. Freeman (2005)
Cancer Res.
65, 2547-2553
|Abstract »|Full Text »|PDF »
The Stress-inducted Proteins RTP801 and RTP801L Are Negative Regulators of the Mammalian Target of Rapamycin Pathway.
M. N. Corradetti, K. Inoki, and K.-L. Guan (2005)
J. Biol. Chem.
280, 9769-9772
|Abstract »|Full Text »|PDF »
Phosphatidylinositol 3-kinase mutations identified in human cancer are oncogenic.
