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Growth Factor-Dependent and -Independent Activation of mTORC2

Jonas R Knudsen1, Andreas M Fritzen1, David E James2

  • 1Section of Molecular Physiology, Department of Nutrition, Exercise and Sports, Faculty of Science, University of Copenhagen, Copenhagen, Denmark.

Trends in Endocrinology and Metabolism: TEM
|November 9, 2019
PubMed

Insights

Mammalian target of rapamycin complex 2 (mTORC2) phosphorylates Akt, a key step in insulin signaling. This review explores mTORC2

Area of Science:

  • Cellular signaling pathways
  • Molecular biology
  • Biochemistry

Background:

  • The target of rapamycin complex 2 (TORC2) was identified in 2002, with its mammalian homolog, mTORC2, described in 2004.
  • mTORC2 was found to directly phosphorylate Akt at Ser473, identifying the long-sought second insulin-responsive Akt kinase.

Purpose of the Study:

  • To review the subcellular localization of mTORC2 and its relation to activation.
  • To summarize current models of growth factor-mediated mTORC2 activation.
  • To explore novel mechanisms of growth factor-independent mTORC2 activation.

Main Methods:

  • Review of existing scientific literature and experimental evidence.
  • Analysis of data pertaining to mTORC2 localization and function.
  • Synthesis of current understanding and identification of research frontiers.

Main Results:

  • Evidence suggests spatial heterogeneity in mTORC2 localization influences its activation.
  • Growth factors, like insulin, trigger mTORC2 activation through specific signaling pathways.
  • Emerging research focuses on mechanisms driving mTORC2 activation independent of growth factors.

Conclusions:

  • Understanding mTORC2's localization and activation mechanisms is crucial for deciphering its role in cellular processes.
  • Further investigation into growth factor-independent activation pathways will reveal new therapeutic targets.
Keywords:
activation mechanismsexercise.mTORC2subcellular localization

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