The target of rapamycin (TOR) proteins

  1. Brian Raught*,
  2. Anne-Claude Gingras*, and
  3. Nahum Sonenberg
  1. Department of Biochemistry and McGill Cancer Centre, McGill University, 3655 Promenade Sir-William-Osler, Montréal, QC H3G 1Y6 Canada

Abstract

Rapamycin potently inhibits downstream signaling from the target of rapamycin (TOR) proteins. These evolutionarily conserved protein kinases coordinate the balance between protein synthesis and protein degradation in response to nutrient quality and quantity. The TOR proteins regulate (i) the initiation and elongation phases of translation, (ii) ribosome biosynthesis, (iii) amino acid import, (iv) the transcription of numerous enzymes involved in multiple metabolic pathways, and (v) autophagy. Intriguingly, recent studies have also suggested that TOR signaling plays a critical role in brain development, learning, and memory formation.

Footnotes

  • * B.R. and A.-C.G. contributed equally to this report.

  • To whom reprint requests should be addressed. E-mail: nsonen{at}med.mcgill.ca.

  • This paper was presented at the National Academy of Sciences colloquium, “Molecular Kinesis in Cellular Function and Plasticity,” held December 7–9, 2000, at the Arnold and Mabel Beckman Center in Irvine, CA.

  • Abbreviations:
    TOR,
    target of rapamycin;
    FKBP12,
    FK506-binding protein, molecular mass of 12 kDa;
    PI3K,
    phosphoinositide 3-kinase;
    5′TOP,
    5′ terminal oligopyrimidine tract;
    NMDA,
    N-methyl-d-aspartate
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