Architecture of human mTOR complex 1

@article{Aylett2016ArchitectureOH,
  title={Architecture of human mTOR complex 1},
  author={Christopher H. S. Aylett and Evelyn Sauer and Stefan Imseng and Daniel Boehringer and Michael N. Hall and Nenad Ban and Timm Maier},
  journal={Science},
  year={2016},
  volume={351},
  pages={48 - 52}
}
From sensing leucine to metabolic control The mTORC1 protein kinase complex plays central roles in regulating cell growth and metabolism and is implicated in common human diseases such as diabetes and cancer. The level of the amino acid leucine tells an organism a lot about its physiological state, including how much food is available, how much insulin is going to be needed, and whether new muscle mass can be made (see the Perspective by Buel and Blenis). Wolfson et al. identified a biochemical… 
Mechanisms of amino acid sensing by the mTORC1 pathway
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These structures have paved the way for the development of novel compounds targeting mTORC1 through the Sestrin2 and CASTOR1 amino acid-binding pockets, which may have important clinical implications in the context of cancer, diabetes, neurological disorders, and longevity.
Sensors for the mTORC1 pathway regulated by amino acids
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Recently, several sensors of leucine, arginine, and S-adenosylmethionine for the amino acid-stimulated mTORC1 pathway have been coming to light and characterization of these sensors is requisite for understanding how cells adjust amino acid sensing pathways to their different needs.
Regulation of mTORC1-Dependent Growth Signaling by Lysosomal Cholesterol
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Cholesterol, an essential lipid for cellular growth, is identified as a nutrient input that drives mTORC1 recruitment and activation at the lysosomal surface and is suggested to contribute to the metabolic derangement observed in Niemann-Pick Type C (NPC) disease in humans.
Cryo-EM insight into the structure of MTOR complex 1 and its interactions with Rheb and substrates
TLDR
A deep understanding is sought of how MTORC1 interacts with and phosphorylates its best-known substrates—the eIF-4E binding protein/4E-BP, the p70 S6 kinase/S6K1B, and PRAS40/AKT1S1—and how this is inhibited by rapamycin.
Regulation of human mTOR complexes by DEPTOR
TLDR
The multifaceted interplay between DEPTOR and mTOR provides a basis for understanding the divergent roles of DEPTor in physiology and opens new routes for targeting the mTOR-DEPTOR interaction in disease.
The 3.2Å resolution structure of human mTORC2
TLDR
A 3.2 Å resolution cryo-EM reconstruction of mTORC2 reveals entangled folds of the defining Rictor and the substrate-binding SIN1 subunits, and identifies the C-terminal domain of Rictsor as the source of the rapamycin insensitivity of m TORC2, and resolves mechanisms for mtorC2 regulation by complex destabilization.
Architecture of human Rag GTPase heterodimers and their complex with mTORC1
TLDR
Cryo–electron microscopy and crystal structures of RagA/RagC in complex with mTORC1 show the mechanism for this locking and explain how oncogenic hotspot mutations disrupt this process.
Structural Mechanisms of mTORC1 activation by RHEB and inhibition by PRAS40
The mechanistic target of rapamycin complex 1 (mTORC1) controls cell growth and metabolism in response to nutrients, energy levels, and growth factors. It contains the atypical kinase mTOR and the
The 3.2-Å resolution structure of human mTORC2
TLDR
A 3.2-Å resolution cryo-EM reconstruction of mTORC2 reveals entangled folds of the defining Rictor and the substrate-binding SIN1 subunits, identifies the carboxyl-terminal domain of Rictsor as the source of the rapamycin insensitivity of m TORC2, and resolves mechanisms for mTORc2 regulation by complex destabilization.
Lysosomal Regulation of mTORC1 by Amino Acids in Mammalian Cells
TLDR
In this review, recent progress with respect to biochemical and biological findings in the regulation of mTORC1 signaling on the lysosomal membrane by amino acids is summarized.
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