TOR signalling

TOR (target of rapamycin) signalling is a cell signalling pathway. TOR and its mammalian ortholog mTOR are serine-threonine kinases that sense growth factor, nutrient or oxygen status and promote appropriate changes in cell growth and proliferation, cell survival, and protein synthesis. TOR signalling has key roles in cancer and autophagy.


Latest Research and Reviews

News and Comment

  • News & Views |

    Dai and colleagues show that activation of AMPK by glucose starvation leads to phosphorylation of GATOR2 and affects nutrient-dependent activation of mTORC1.

    • Nerea Deleyto-Seldas
    •  & Alejo Efeyan
  • News & Views |

    mTORC1 integrates environmental signals to promote anabolism and repress catabolism. In this issue of Nature Metabolism, Hosios et al. identify a role for mTORC1 in controlling endosomal trafficking and degradation of membrane phospholipids in the lysosome, revealing a novel process used by cells to adapt to poor growth conditions.

    • Laura Tribouillard
    •  & Mathieu Laplante
    Nature Metabolism 4, 1620-1622
  • News & Views |

    The Rag GTPases form the link between extracellular nutrients and the activation of mTORC1. RagA/B and RagC/D have been considered functionally redundant, but two studies now show that each isoform and gene have specific features, making their control of mTORC1 activity more nuanced and complex than previously appreciated.

    • Nicola Alesi
    •  & Elizabeth P. Henske
    Nature Cell Biology 24, 1330-1331
  • News & Views |

    Ong et al. uncover a role for the YAP/TAZ–TEAD transcriptional pathways in retinal angiogenesis via the regulation of amino acid transporters and assessed mTORC activation. These findings establish the mechanism through which endothelial cells regulate nutrient acquisition and consumption.

    • Roxana E. Oberkersch
    •  & Massimo M. Santoro
    Nature Metabolism 4, 645-646
  • News & Views |

    Nutrient availability and the cell cycle are known to affect chromatin accessibility. A fundamental question is which mechanisms are involved in connecting nutrient levels, the cell cycle and chromatin regulation. In this issue, Zhang et al. reveal a signalling cascade whereby nutrient-sensing mTORC1 activates the cell-cycle regulator CDK2, thus leading to nuclear translocation of the metabolic enzyme triosephosphate isomerase 1 (TPI1). In the nucleus, TPI1 alters the levels of acetate and global histone acetylation through the metabolite dihydroxyacetone phosphate.

    • Lara Roach
    •  & Raul Mostoslavsky
    Nature Metabolism 3, 729-731