mTOR coordinates protein synthesis, mitochondrial activity and proliferation

Cell Cycle. 2015;14(4):473-80. doi: 10.4161/15384101.2014.991572.


Protein synthesis is one of the most energy consuming processes in the cell. The mammalian/mechanistic target of rapamycin (mTOR) is a serine/threonine kinase that integrates a multitude of extracellular signals and intracellular cues to drive growth and proliferation. mTOR activity is altered in numerous pathological conditions, including metabolic syndrome and cancer. In addition to its well-established role in regulating mRNA translation, emerging studies indicate that mTOR modulates mitochondrial functions. In mammals, mTOR coordinates energy consumption by the mRNA translation machinery and mitochondrial energy production by stimulating synthesis of nucleus-encoded mitochondria-related proteins including TFAM, mitochondrial ribosomal proteins and components of complexes I and V. In this review, we highlight findings that link mTOR, mRNA translation and mitochondrial functions.

Keywords: 4E-BP1; TCA cycle; eIF4E; mRNA translation; mTOR; metabolism; mitochondria; oxidative phosphorylation.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Cell Proliferation / physiology*
  • Humans
  • Mitochondria / physiology*
  • Models, Biological*
  • Protein Biosynthesis / physiology*
  • Signal Transduction / physiology*
  • TOR Serine-Threonine Kinases / physiology*


  • TOR Serine-Threonine Kinases