New insights into mTOR signaling: mTORC2 and beyond
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Updated: Jun 23, 2026

Isolation of Primary Mouse Hepatocytes for Nascent Protein Synthesis Analysis by Non-radioactive L-azidohomoalanine Labeling Method
Published on: October 23, 2018
Dario R Alessi1, Laura R Pearce, Juan M García-Martínez
1MRC Protein Phosphorylation Unit, College of Life Sciences, University of Dundee, Dow Street, Dundee DD15EH, Scotland, UK. d.r.alessi@dundee.ac.uk
Abstract:
The mammalian target of rapamycin complex 2 (mTORC2) plays critical roles in regulating cell growth and proliferation. mTORC2 promotes the activation of the serum glucocorticoid-induced protein kinase (SGK). This mTOR complex also promotes the constitutive phosphorylation of proline-directed serine or threonine sites in the turn motif of Akt and protein kinase C isoforms. mTORC2 may control phosphorylation of the turn motif by promoting the activity of a kinase that targets the Ser/Thr-Pro sequence or by inhibiting the activity of a phosphatase.
Insights
Mammalian target of rapamycin complex 2 (mTORC2) regulates cell growth and proliferation. It activates SGK and phosphorylates Akt and PKC isoforms, potentially by influencing kinase or phosphatase activity.
Area of Science:
- Cellular Biology
- Molecular Biology
- Biochemistry
Background:
- The mammalian target of rapamycin complex 2 (mTORC2) is a crucial regulator of cell growth and proliferation.
- mTORC2 influences key signaling pathways involved in cell survival and metabolism.
Purpose of the Study:
- To elucidate the regulatory mechanisms of mTORC2 in cell growth and proliferation.
- To understand mTORC2's role in the activation of downstream kinases like SGK, Akt, and protein kinase C (PKC) isoforms.
Main Methods:
- Investigating the effects of mTORC2 on serum glucocorticoid-induced protein kinase (SGK) activation.
- Analyzing the phosphorylation status of specific serine/threonine sites in Akt and PKC isoforms.
- Exploring the potential involvement of kinases and phosphatases in mediating mTORC2-dependent phosphorylation.
Main Results:
- mTORC2 was found to promote the activation of SGK.
- Constitutive phosphorylation of proline-directed serine or threonine sites in the turn motif of Akt and PKC isoforms was observed.
- Evidence suggests mTORC2 may regulate this phosphorylation by modulating kinase or phosphatase activity.
Conclusions:
- mTORC2 plays a significant role in cellular processes through the regulation of SGK, Akt, and PKC.
- The findings provide insights into the molecular mechanisms by which mTORC2 controls cell growth and proliferation.
- Further research is warranted to fully delineate the kinase-phosphatase interplay in mTORC2 signaling.
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