Growth Factor-Dependent and -Independent Activation of mTORC2.

The target of rapamycin complex 2 (TORC2) was discovered in 2002 in budding yeast. Its mammalian counterpart, mTORC2, was first described in 2004. Soon thereafter it was demonstrated that mTORC2 directly phosphorylates Akt on Ser473, ending a long search for the elusive 'second' insulin-responsive Akt kinase. In this review we discuss key evidence pertaining to the subcellular localization of mTORC2, highlighting a spatial heterogeneity that relates to mTORC2 activation. We summarize current models for how growth factors (GFs), such as insulin, trigger mTORC2 activation, and we provide a comprehensive discussion focusing on a new exciting frontier, the molecular mechanisms underpinning GF-independent activation of mTORC2. Copyright © 2019 Elsevier Ltd. All rights reserved.

Citation

Jonas R Knudsen, Andreas M Fritzen, David E James, Thomas E Jensen, Maximilian Kleinert, Erik A Richter. Growth Factor-Dependent and -Independent Activation of mTORC2. Trends in endocrinology and metabolism: TEM. 2020 Jan;31(1):13-24

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PMID: 31699566

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