Regulation of mTORC1 by growth factors, energy status, amino acids and mechanical stimuli at a glance

J Int Soc Sports Nutr. 2016 Mar 1:13:8. doi: 10.1186/s12970-016-0118-y. eCollection 2016.

Abstract

The mechanistic/mammalian target of rapamycin complex 1 (mTORC1) plays a pivotal role in the regulation of skeletal muscle protein synthesis. Activation of the complex leads to phosphorylation of two important sets of substrates, namely eIF4E binding proteins and ribosomal S6 kinases. Phosphorylation of these substrates then leads to an increase in protein synthesis, mainly by enhancing translation initiation. mTORC1 activity is regulated by several inputs, such as growth factors, energy status, amino acids and mechanical stimuli. Research in this field is rapidly evolving and unraveling how these inputs regulate the complex. Therefore this review attempts to provide a brief and up-to-date narrative on the regulation of this marvelous protein complex. Additionally, some sports supplements which have been shown to regulate mTORC1 activity are discussed.

Keywords: Akt; Muscle protein synthesis; Myostatin; mTORC1.

Publication types

  • Review

MeSH terms

  • AMP-Activated Protein Kinases
  • Active Transport, Cell Nucleus / drug effects
  • Amino Acids / metabolism
  • Animals
  • Dietary Supplements*
  • Growth Hormone
  • Humans
  • Intracellular Signaling Peptides and Proteins
  • Mechanistic Target of Rapamycin Complex 1
  • Multiprotein Complexes / metabolism*
  • Muscle Proteins / biosynthesis*
  • Muscle Proteins / metabolism
  • Muscle, Skeletal / drug effects
  • Muscle, Skeletal / metabolism*
  • Phosphorylation
  • Protein Binding
  • Protein Biosynthesis / drug effects
  • Signal Transduction
  • TOR Serine-Threonine Kinases / metabolism*

Substances

  • Amino Acids
  • Intracellular Signaling Peptides and Proteins
  • Multiprotein Complexes
  • Muscle Proteins
  • Growth Hormone
  • Mechanistic Target of Rapamycin Complex 1
  • TOR Serine-Threonine Kinases
  • AMP-Activated Protein Kinases