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

Publication TypeJournal Article
AuthorsFrias, MA, Thoreen CC, Jaffe JD, Schroder W., Sculley T., Carr SA, and Sabatini DM
AbstractThe 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.
Year of Publication2006
JournalCurrent biology : CB
Volume16
Issue18
Pages1865-70
Date Published (YYYY/MM/DD)2006/09/19
ISSN Number0960-9822
DOI10.1016/j.cub.2006.08.001
PubMedhttp://www.ncbi.nlm.nih.gov/pubmed/16919458?dopt=Abstract