Premium
The mammalian target of rapamycin in translation and folding
Author(s) -
Jacinto Estela,
Oh Wonjun,
Wu Changchih,
Facchinetti Valeria,
Su Bing
Publication year - 2010
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.24.1_supplement.187.3
Subject(s) - mtorc2 , pi3k/akt/mtor pathway , mtorc1 , microbiology and biotechnology , mechanistic target of rapamycin , phosphorylation , protein kinase b , biology , rptor , translation (biology) , signal transduction , genetics , gene , messenger rna
Cell growth requires the synthesis of proteins and other macromolecules that are critical for increase in cellular mass and number. The mammalian target of rapamycin (mTOR) controls cell growth by regulating various aspects of protein synthesis. mTOR, in association with raptor and mLST8 (termed mTOR complex 1 or mTORC1), regulates translation in a rapamycin‐sensitive manner. mTOR also forms a structurally distinct complex with rictor, SIN1, and mLST8 (termed mTORC2). The function of mTORC2 and why this complex is insensitive to rapamycin are currently poorly understood. So far it is known that mTORC2 is involved in actin cytoskeleton reorganization and phosphorylation of Akt/PKB, an AGC kinase family member that becomes deregulated in cancer. Recently, we found that mTORC2 controls the folding and stability of Akt and conventional PKC by phosphorylation at the highly conserved turn motif site. This TORC2 function is growth factor‐independent and conserved from yeast to mammals. We will discuss how mTOR may function to link translation to protein folding. Our findings reveal the diversity of mTOR functions in the control of protein synthesis and cell growth. This work was supported in part by the American Heart Association 0530192N, American Cancer Society RSG0721601TBE, and NIH GM079176 (to E.J.) and NIH HL070225 (to B.S.)