Our hosting provider will be performing UPS maintenance on Tuesday, Oct 25, 2016 between 8 AM and 5 PM PDT. SciCrunch searching services will be down during this time.

Preparing your results

Our searching services are busy right now. Your search will reload in five seconds.

Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.

Selective ATP-competitive inhibitors of TOR suppress rapamycin-insensitive function of TORC2 in Saccharomyces cerevisiae.


The target of rapamycin (TOR) is a critical regulator of growth, survival, and energy metabolism. The allosteric TORC1 inhibitor rapamycin has been used extensively to elucidate the TOR related signal pathway but is limited by its inability to inhibit TORC2. We used an unbiased cell proliferation assay of a kinase inhibitor library to discover QL-IX-55 as a potent inhibitor of S. cerevisiae growth. The functional target of QL-IX-55 is the ATP-binding site of TOR2 as evidenced by the discovery of resistant alleles of TOR2 through rational design and unbiased selection strategies. QL-IX-55 is capable of potently inhibiting both TOR complex 1 and 2 (TORC1 and TORC2) as demonstrated by biochemical IP kinase assays (IC(50) <50 nM) and cellular assays for inhibition of substrate YPK1 phosphorylation. In contrast to rapamycin, QL-IX-55 is capable of inhibiting TORC2-dependent transcription, which suggests that this compound will be a powerful probe to dissect the Tor2/TORC2-related signaling pathway in yeast.

Pubmed ID: 22496512


  • Liu Q
  • Ren T
  • Fresques T
  • Oppliger W
  • Niles BJ
  • Hur W
  • Sabatini DM
  • Hall MN
  • Powers T
  • Gray NS


ACS chemical biology

Publication Data

June 15, 2012

Associated Grants

  • Agency: NHGRI NIH HHS, Id: HG006097
  • Agency: NIGMS NIH HHS, Id: R01GM86387
  • Agency: PHS HHS, Id: U54 A1057159
  • Agency: NHGRI NIH HHS, Id: U54 HG006097
  • Agency: NHGRI NIH HHS, Id: U54 HG006097-01
  • Agency: NHGRI NIH HHS, Id: U54 HG006097-01S1

Mesh Terms

  • Adenosine Triphosphate
  • Antifungal Agents
  • Cell Cycle Proteins
  • Humans
  • Models, Molecular
  • Mycoses
  • Phosphatidylinositol 3-Kinases
  • Protein Kinase Inhibitors
  • Protein-Serine-Threonine Kinases
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Signal Transduction
  • Sirolimus
  • Transcription Factors