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Essential function of TORC2 in PKC and Akt turn motif phosphorylation, maturation and signalling
Author(s) -
Ikenoue Tsuneo,
Inoki Ken,
Yang Qian,
Zhou Xiaoming,
Guan KunLiang
Publication year - 2008
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1038/emboj.2008.119
Subject(s) - phosphorylation , mtorc2 , protein kinase b , microbiology and biotechnology , biology , pi3k/akt/mtor pathway , protein kinase c , signal transduction , mtorc1
Protein kinase C (PKC) is involved in a wide array of cellular processes such as cell proliferation, differentiation and apoptosis. Phosphorylation of both turn motif (TM) and hydrophobic motif (HM) are important for PKC function. Here, we show that the mammalian target of rapamycin complex 2 (mTORC2) has an important function in phosphorylation of both TM and HM in all conventional PKCs, novel PKCε as well as Akt. Ablation of mTORC2 components (Rictor, Sin1 or mTOR) abolished phosphorylation on the TM of both PKCα and Akt and HM of Akt and decreased HM phosphorylation of PKCα. Interestingly, the mTORC2‐dependent TM phosphorylation is essential for PKCα maturation, stability and signalling. Our study demonstrates that mTORC2 is involved in post‐translational processing of PKC by facilitating TM and HM phosphorylation and reveals a novel function of mTORC2 in cellular regulation.