What controls TOR?

@article{Jacinto2008WhatCT,
  title={What controls TOR?},
  author={Estela Jacinto},
  journal={IUBMB Life},
  year={2008},
  volume={60}
}
  • E. Jacinto
  • Published 1 August 2008
  • Biology
  • IUBMB Life
The target of rapamycin (TOR) is a protein kinase with numerous functions in cell growth control. Some of these functions can be potently inhibited by rapamycin, an immunosuppressive and potential anticancer drug. TOR exists as part of two functionally distinct protein complexes. The functions of TOR complex 1 (TORC1) are effectively inhibited by rapamycin, but the mechanism for this inhibition remains elusive. The identification of TORC2 and recent reports that rapamycin can inhibit TORC2… 
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The Target of Rapamycin: Structure and Functions
TLDR
Inhibition of m TOR activity using rapamycin and more recently via mTOR active site inhibitors and disruption of mTOR complexes, has revealed important insights on how mTOR functions under physiological and pathological conditions.
Regulation of TOR Complex 1 by Amino Acids Through Small GTPases
mTOR Ser-2481 Autophosphorylation Monitors mTORC-specific Catalytic Activity and Clarifies Rapamycin Mechanism of Action*
TLDR
This work re-examines the regulation of mTOR Ser-2481 autophosphorylation in vivo by studying mTORC-specific Ser(P)-2481 in m TORC1 andmTORC2, with a primary focus on mTOR C1.
mTORC1‐ and mTORC2‐interacting proteins keep their multifunctional partners focused
TLDR
The actions of mTOR are reviewed with emphasis on the controlling role of m TORC1 and mTORC2‐interacting proteins and highlight the mechanisms linked to cell migration.
AGC Kinases in mTOR Signaling
Evolutionary conservation of TORC1 components, TOR, Raptor, and LST8, between rice and yeast
TLDR
Analysis of the gene structure and functions of TORC components in rice and implementation tests of rice TOR (OsTOR) components in yeast showed that chimeric TOR, which consisted of the HEAT repeat and FAT domain from yeast and other regions from rice, rescued the tor mutants, indicating the importance of the N-terminal region of the TOR, HEAT, and FAT domains for functional diversification of theTOR complex.
mTORC1-Activated S6K1 Phosphorylates Rictor on Threonine 1135 and Regulates mTORC2 Signaling
TLDR
It is shown that growth factors promote the phosphorylation of Rictor (rapamycin-insensitive companion of mTOR), an essential subunit of m TORC2, and a new regulatory link between the two mTOR complexes is uncovered, whereby RictOr integrates mTORC1-dependent signaling.
Mammalian Target of Rapamycin Complex 1 (mTORC1) Plays a Role in Pasteurella multocida Toxin (PMT)-induced Protein Synthesis and Proliferation in Swiss 3T3 Cells*
TLDR
The findings reveal for the first time that PMT activates mTORC1 through the Gαq/11/PLCβ/PKC pathway, and the fact thatPMT-induced protein synthesis and cell migration is partially inhibited by rapamycin indicates that these processes are in part mediated by the m TORC1 pathway.
ERK1/2 Phosphorylate Raptor to Promote Ras-dependent Activation of mTOR Complex 1 (mTORC1)*
TLDR
The data provide a novel regulatory mechanism by which mitogenic and oncogenic activation of the Ras/MAPK pathway promotes mTOR signaling, and three proline-directed residues within Raptor, Ser8, Ser696, and Ser863, which are directly phosphorylated by ERK1/2 are found.
Site-Specific mTOR Phosphorylation Promotes mTORC1-Mediated Signaling and Cell Growth
TLDR
This work identifies a new site of mTOR phosphorylation (S1261) by tandem mass spectrometry and demonstrates that insulin-phosphatidylinositol 3-kinase signaling promotes mTOR S1261osphorylation in both m TORC1 and mTORC2, and suggests a model whereby insulin-stimulated mTOR s1261 phosphorylated promotes mtorC1 autokinase activity, substrate phosphorylations, and cell growth.
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References

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TLDR
It is demonstrated that mammalian TOR is also oligomeric, likely a TORC2-TORC2 dimer, and the architecture of TorC2 is discussed in the context of TORC 2 assembly and regulation.
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TLDR
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TLDR
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TLDR
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