April 13, 2021Science SignalingOpen Access

mTORC2 controls the activity of PKC and Akt by phosphorylating a conserved TOR interaction motif

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Phosphorylation of an evolutionarily conserved motif by mTORC2 directly enables the maturation and activation of AGC kinases, including the critical signaling enzymes PKC and Akt.
Biochemical investigation demonstrates that mTORC2 regulates enzymatic activity by targeting the conserved TOR interaction motif shared across these essential cellular kinases.
Highlights a foundational mechanism for AGC kinase maturation, suggesting that mTORC2-driven phosphorylation is essential for cellular signaling; further preclinical work needed.

Implication

Molecular analysis demonstrates that mTORC2 phosphorylates a conserved motif in AGC kinases, indicating a vital mechanism controlling PKC and Akt activity.

Abstract

Phosphorylation of an evolutionarily conserved motif by mTORC2 enables the maturation of AGC kinases.

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Cite This Study

Baffi et al. (2021) studied this question.

synapsesocial.com/papers/690cc2e631132aecb62f137c https://doi.org/10.1126/scisignal.abe4509

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Implication

Molecular analysis demonstrates that mTORC2 phosphorylates a conserved motif in AGC kinases, indicating a vital mechanism controlling PKC and Akt activity.

Abstract

Phosphorylation of an evolutionarily conserved motif by mTORC2 enables the maturation of AGC kinases.

mTORC2 controls the activity of PKC and Akt by phosphorylating a conserved TOR interaction motif

Key Points

Implication

Abstract

Discussion

Cite This Study

mTORC2 controls the activity of PKC and Akt by phosphorylating a conserved TOR interaction motif

Key Points

Implication

Abstract

Discussion

Cite This Study

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