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Science 332 (6035): 1270-1271

Copyright © 2011 by the American Association for the Advancement of Science

New mTOR Targets Grb Attention

Sung Su Yea1, and David A. Fruman2

A cellular enzyme called mechanistic (or mammalian) target of rapamycin (mTOR) controls cell growth and division, and is an important drug target in cancer (1). Despite extensive study, a complete understanding of mTOR function has remained elusive. One reason is that rapamycin, the natural compound that led to the identification of mTOR, only partially inhibits the enzyme. In addition, mTOR functions in two distinct protein complexes (mTORC1 and mTORC2). Furthermore, only a few proteins have been identified as mTOR substrates, and these seem insufficient to explain its myriad functions. Two papers in this issue, by Hsu et al. on page 1317 (2) and Yu et al. on page 1322 (3), uncover dozens of new substrates and downstream targets of mTOR through proteomic screens. These results have major implications for research and drug development in cancer and metabolic disorders.

1 Department of Biochemistry, College of Medicine, Inje University, Busan 614-735, Korea.
2 Department of Molecular Biology and Biochemistry, University of California, Irvine, Irvine, CA 92697, USA.

E-mail: dfruman{at}

VS-5584, a Novel and Highly Selective PI3K/mTOR Kinase Inhibitor for the Treatment of Cancer.
S. Hart, V. Novotny-Diermayr, K. C. Goh, M. Williams, Y. C. Tan, L. C. Ong, A. Cheong, B. K. Ng, C. Amalini, B. Madan, et al. (2013)
Mol. Cancer Ther. 12, 151-161
   Abstract »    Full Text »    PDF »
Regulation of mRNA Translation by Signaling Pathways.
P. P. Roux and I. Topisirovic (2012)
Cold Spring Harb Perspect Biol 4, a012252
   Abstract »    Full Text »    PDF »
Structure-Activity Analysis of Niclosamide Reveals Potential Role for Cytoplasmic pH in Control of Mammalian Target of Rapamycin Complex 1 (mTORC1) Signaling.
B. D. Fonseca, G. H. Diering, M. A. Bidinosti, K. Dalal, T. Alain, A. D. Balgi, R. Forestieri, M. Nodwell, C. V. Rajadurai, C. Gunaratnam, et al. (2012)
J. Biol. Chem. 287, 17530-17545
   Abstract »    Full Text »    PDF »
Structural Basis for Activation and Inhibition of Class I Phosphoinositide 3-Kinases.
O. Vadas, J. E. Burke, X. Zhang, A. Berndt, and R. L. Williams (2011)
Science Signaling 4, re2
   Abstract »    Full Text »    PDF »

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