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Sci. Signal., 27 March 2012
Vol. 5, Issue 217, p. pe12
[DOI: 10.1126/scisignal.2003026]

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Deconvolution of mTORC2 "in Silico"

Diane C. Fingar1* and Ken Inoki2,3,4*

1 Department of Cell and Developmental Biology, University of Michigan, Ann Arbor, MI 48109, USA.
2 Life Sciences Institute, University of Michigan, Ann Arbor, MI 48109, USA.
3 Department of Molecular and Integrative Physiology, University of Michigan, Ann Arbor, MI 48109, USA.
4 Department of Internal Medicine, University of Michigan, Ann Arbor, MI 48109, USA.

Abstract: The protein kinase mTOR (mammalian or mechanistic target of rapamycin) coordinates a complex signal transduction network. By assembling with unique and shared partner proteins, mTOR forms the catalytic core of at least two complexes, mTOR complex 1 (mTORC1) and mTORC2, that show differential sensitivity to the allosteric mTOR inhibitor rapamycin and that phosphorylate distinct substrates to modulate cell growth, proliferation, survival, and metabolism in response to diverse environmental cues. Understanding mTOR network circuitry will provide insight into how its deregulation contributes to pathologic states such as diabetes, cancer, and cardiovascular disease. Research published in Science Signaling describes an investigation of the complex insulin-mTOR network by combining classic biochemical approaches with dynamic mathematical modeling in silico to elucidate how insulin activates mTORC2, an event that remains poorly defined.

* Corresponding authors. E-mail: dfingar{at}umich.edu (D.C.F.); inokik{at}umich.edu (K.I.)

Citation: D. C. Fingar, K. Inoki, Deconvolution of mTORC2 "in Silico". Sci. Signal. 5, pe12 (2012).

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THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Response to Comment on "A Dynamic Network Model of mTOR Signaling Reveals TSC-Independent mTORC2 Regulation": Building a Model of the mTOR Signaling Network with a Potentially Faulty Tool.
P. Dalle Pezze, A. G. Sonntag, D. P. Shanley, and K. Thedieck (2012)
Science Signaling 5, lc4
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