Molecular mechanisms relating to amino acid regulation of protein synthesis

Nutr Res Rev. 2019 Dec;32(2):183-191. doi: 10.1017/S0954422419000052. Epub 2019 May 17.

Abstract

Some amino acids (AA) act through several signalling pathways and mechanisms to mediate the control of gene expression at the translation level, and the regulation occurs, specifically, on the initiation and the signalling pathways for translation. The translation of mRNA to protein synthesis proceeds through the steps of initiation and elongation, and AA act as important feed-forward activators that are involved in many pathways, such as the sensing and the transportation of AA by cells, in these steps in many tissues of mammals. For the translation, phosphorylation of eukaryotic translation initiation factor 2α (eIF2α) is a critical molecule that controls the translation initiation and its functions can be regulated by some AA. Another control point in the mRNA binding step in the translation initiation is at the regulation by mammalian target of rapamycin, which requires a change of phosphorylation status of ribosomal protein S6. In fact, the change of phosphorylation status of ribosomal protein S6 might be involved in global protein synthesis. The present review summarises recent work on the molecular mechanisms of the regulation of protein synthesis by AA and highlights new findings.

Keywords: Amino acids; Mammalian target of rapamycin (mTOR); Protein synthesis; eEF2; eIF2.

Publication types

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

MeSH terms

  • Amino Acids / physiology*
  • Animals
  • Arginine / pharmacology
  • Gene Expression Regulation / drug effects
  • Gene Expression Regulation / physiology*
  • Leucine / pharmacology
  • Peptide Chain Elongation, Translational / physiology
  • Phosphorylation / physiology
  • Protein Biosynthesis / genetics*
  • RNA, Messenger / genetics
  • Ribosomal Protein S6 / physiology
  • Signal Transduction / physiology
  • TOR Serine-Threonine Kinases / chemistry
  • TOR Serine-Threonine Kinases / physiology
  • eIF-2 Kinase / physiology

Substances

  • Amino Acids
  • RNA, Messenger
  • Ribosomal Protein S6
  • Arginine
  • TOR Serine-Threonine Kinases
  • eIF-2 Kinase
  • Leucine