Molecular mechanisms relating to amino acid regulation of protein synthesis.

Nutr Res Rev

College of Animal Science and Technology, Northwest A&F University, Yangling Shaanxi, 712100, People's Republic of China.

Published: December 2019

AI Article Synopsis

  • Amino acids play a vital role in controlling gene expression at the translation level by influencing initiation processes and various signaling pathways.
  • The translation process involves steps like initiation and elongation, with amino acids acting as key activators that assist in their sensing and transportation within cells.
  • Critical regulators, such as the phosphorylation of eIF2α and ribosomal protein S6, significantly impact translation initiation, demonstrating the complex relationships between amino acids and protein synthesis.

Article 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.

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Source
http://dx.doi.org/10.1017/S0954422419000052DOI Listing

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