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Nutr Res Rev. 2019 May 17:1-9. doi: 10.1017/S0954422419000052. [Epub ahead of print]

Molecular mechanisms relating to amino acid regulation of protein synthesis.

Author information

1
College of Animal Science and Technology,Northwest A&F University,Yangling Shaanxi,712100,People's Republic of China.
2
Institute of Agriculture,University of Western Australia,Crawley,WA 6009,Australia.

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:

4EBP1 inhibitory 4E-binding protein-1; AA amino acid; Arg arginine; GCN2 general control nonderepressible 2; Ile isoleucine; Leu leucine; MAP4K3 mitogen-activated protein kinase 3; Met methionine; Rag Ras-related GTP-binding protein; Rheb Ras homologue enriched in brain; S6K1 S6 kinase 1; TSC tuberous sclerosis complex; Thr threonine; Trp tryptophan; Val valine; Vps34 vacuolar protein sorting 34; eEF eukaryotic translation elongation factor; eIF eukaryotic initiation factor; mTOR mammalian target of rapamycin; mTORC1 mammalian target of rapamycin complex 1; mTORC2 mammalian target of rapamycin complex 2; Amino acids; Mammalian target of rapamycin (mTOR); Protein synthesis; eEF2; eIF2

PMID:
31097041
DOI:
10.1017/S0954422419000052

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