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MTORC2 phosphorylates protein kinase C? to regulate its stability and activity.


ABSTRACT: Protein kinase C? (PKC?) is phosphorylated at the activation loop and the turn motif (TM). However, the TM kinase and functional relevance of TM phosphorylation remain largely unknown. We demonstrate that PKC? TM is phosphorylated directly by the mTORC2 complex, and this phosphorylation is required for maintaining PKC? kinase activity and stability. Functionally, mTORC2 regulates the activity of Rho family of GTPases, and therefore the organization of the actin cytoskeleton, through the control of PKC? activity. Taken together, our findings identify PKC? as a novel substrate and downstream effector of mTORC2 signaling.

SUBMITTER: Li X 

PROVIDER: S-EPMC3989865 | biostudies-other | 2014 Feb

REPOSITORIES: biostudies-other

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mTORC2 phosphorylates protein kinase Cζ to regulate its stability and activity.

Li Xin X   Gao Tianyan T  

EMBO reports 20131227 2


Protein kinase Cζ (PKCζ) is phosphorylated at the activation loop and the turn motif (TM). However, the TM kinase and functional relevance of TM phosphorylation remain largely unknown. We demonstrate that PKCζ TM is phosphorylated directly by the mTORC2 complex, and this phosphorylation is required for maintaining PKCζ kinase activity and stability. Functionally, mTORC2 regulates the activity of Rho family of GTPases, and therefore the organization of the actin cytoskeleton, through the control  ...[more]

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