Curr Biol 2006,
PMID: 16919458
Frias, Maria A; Thoreen, Carson C; Jaffe, Jacob D; Schroder, Wayne; Sculley, Tom; Carr, Steven A; Sabatini, David M
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.
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Text Mining Data
Dashed line = No text mining data
Manually curated Databases
-
IRef Biogrid Interaction:
RICTOR
—
MTOR
(physical association, affinity chromatography technology)
-
IRef Biogrid Interaction:
RPTOR
—
MTOR
(physical association, affinity chromatography technology)
-
IRef Innatedb Interaction:
MLST8
—
MTOR
(unknown, -)
-
NCI Pathway Database Class I PI3K signaling events mediated by Akt:
mTORC2 complex (MTOR-RICTOR-MLST8-MAPKAP1)
→
AKT1 (AKT1)
(modification, activates)
Evidence: mutant phenotype, assay, physical interaction, other species
-
NCI Pathway Database mTOR signaling pathway:
mTORC2 complex (MTOR-MLST8-RICTOR-MAPKAP1-PRR5)
→
AKT1 (AKT1)
(modification, activates)
Evidence: mutant phenotype, assay, physical interaction
In total, 16 gene pairs are associated to this article in curated databases