Two TOR complexes, only one of which is rapamycin sensitive, have distinct roles in cell growth control

Robbie Loewith, Estela Jacinto, Stephan Wullschleger, Anja Lorberg, José L. Crespo, Débora Bonenfant, Wolfgang Oppliger, Paul Jenoe, Michael N. Hall

Research output: Contribution to journalArticlepeer-review

1328 Scopus citations

Abstract

The target of rapamycin (TOR) proteins in Saccharomyces cerevisiae, TOR1 and TOR2, redundantly regulate growth in a rapamycin-sensitive manner. TOR2 additionally regulates polarization of the actin cytoskeleton in a rapamycin-insensitive manner. We describe two functionally distinct TOR complexes. TOR Complex 1 (TORC1) contains TOR1 or TOR2, KOG1 (YHR186c), and LST8. TORC2 contains TOR2, AVO1 (YOL078w), AVO2 (YMR068w), AVO3 (YER093c), and LST8. FKBP-rapamycin binds TORC1, and TORC1 disruption mimics rapamycin treatment, suggesting that TORC1 mediates the rapamycin-sensitive, TOR-shared pathway. FKBP-rapamycin fails to bind TORC2, and TORC2 disruption causes an actin defect, suggesting that TORC2 mediates the rapamycin-insensitive, TOR2-unique pathway. Thus, the distinct TOR complexes account for the diversity, specificity, and selective rapamycin inhibition of TOR signaling. TORC1 and possibly TORC2 are conserved from yeast to man.

Original languageEnglish (US)
Pages (from-to)457-468
Number of pages12
JournalMolecular cell
Volume10
Issue number3
DOIs
StatePublished - Sep 1 2002
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Cell Biology

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