Complexity of the TOR signaling network

Trends Cell Biol. 2006 Apr;16(4):206-12. doi: 10.1016/j.tcb.2006.02.002. Epub 2006 Mar 3.

Abstract

The target of rapamycin (TOR) is a serine/threonine kinase of the phosphatidylinositol kinase-related kinase family and is highly conserved from yeast to mammals. TOR functions as a central regulator of cell growth and is itself regulated by a wide range of signals, including growth factors, nutrients and stress conditions. Recent studies in eukaryotic cells have identified two distinct TOR complexes, TORC1 and TORC2, which phosphorylate different substrates and have distinct physiological functions. Here, we discuss new findings that have extended the complexity of TOR signaling and the different roles of the TORC complexes in yeast, flies and mammals.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Animals
  • Cell Communication*
  • Cell Enlargement
  • Drosophila Proteins / metabolism*
  • Models, Biological
  • Multiprotein Complexes / metabolism
  • Phosphatidylinositol 3-Kinases / metabolism*
  • Protein Kinases / metabolism*
  • Protein-Serine-Threonine Kinases
  • Saccharomyces cerevisiae Proteins / metabolism*
  • Signal Transduction*
  • TOR Serine-Threonine Kinases

Substances

  • Drosophila Proteins
  • Multiprotein Complexes
  • Saccharomyces cerevisiae Proteins
  • Protein Kinases
  • Phosphatidylinositol 3-Kinases
  • target of rapamycin protein, Drosophila
  • TOR Serine-Threonine Kinases
  • Protein-Serine-Threonine Kinases
  • target of rapamycin protein, S cerevisiae