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mSin1 is necessary for Akt/PKB phosphorylation, and its isoforms define three distinct mTORC2s.

The mammalian target of rapamycin (mTOR) is a serine/threonine kinase that participates in at least two distinct multiprotein complexes, mTORC1 and mTORC2 . These complexes play important roles in the regulation of cell growth, proliferation, survival, and metabolism. mTORC2 is a hydrophobic motif kinase for the cell-survival protein Akt/PKB and, here, we identify mSin1 as a component of mTORC2 but not mTORC1. mSin1 is necessary for the assembly of mTORC2 and for its capacity to phosphorylate Akt/PKB. Alternative splicing generates at least five isoforms of the mSin1 protein , three of which assemble into mTORC2 to generate three distinct mTORC2s. Even though all mTORC2s can phosphorylate Akt/PKB in vitro, insulin regulates the activity of only two of them. Thus, we propose that cells contain several mTORC2 flavors that may phosphorylate Akt/PKB in response to different signals.

Pubmed ID: 16919458


  • Frias MA
  • Thoreen CC
  • Jaffe JD
  • Schroder W
  • Sculley T
  • Carr SA
  • Sabatini DM


Current biology : CB

Publication Data

September 19, 2006

Associated Grants

  • Agency: NIAID NIH HHS, Id: R01 AI047389
  • Agency: NCI NIH HHS, Id: R01 CA103866

Mesh Terms

  • Adaptor Proteins, Signal Transducing
  • Cell Line, Tumor
  • Humans
  • Insulin
  • Phosphorylation
  • Protein Binding
  • Protein Isoforms
  • Protein Kinases
  • Proto-Oncogene Proteins c-akt
  • Sirolimus
  • TOR Serine-Threonine Kinases