Protein Post-Translational Modifications Based on Proteomics: A Potential Regulatory Role in Animal Science

J Agric Food Chem. 2024 Mar 27;72(12):6077-6088. doi: 10.1021/acs.jafc.3c08332. Epub 2024 Mar 19.

Abstract

Genomic studies in animal breeding have provided a wide range of references; however, it is important to note that genes and mRNA alone do not fully capture the complexity of living organisms. Protein post-translational modification, which involves covalent modifications regulated by genetic and environmental factors, serves as a fundamental epigenetic mechanism that modulates protein structure, activity, and function. In this review, we comprehensively summarize various phosphorylation and acylation modifications on metabolic enzymes relevant to energy metabolism in animals, including acetylation, succinylation, crotonylation, β-hydroxybutylation, acetoacetylation, and lactylation. It is worth noting that research on animal energy metabolism and modification regulation lags behind the demands for growth and development in animal breeding compared to human studies. Therefore, this review provides a novel research perspective by exploring unreported types of modifications in livestock based on relevant findings from human or animal models.

Keywords: acylation; animal breeding; enzymatic modification; epigenetics; lysine modification; phosphorylation; post-translational modification; β-hydroxybutylation.

Publication types

  • Review

MeSH terms

  • Acetylation
  • Acylation
  • Animals
  • Humans
  • Protein Processing, Post-Translational
  • Proteins* / metabolism
  • Proteomics*

Substances

  • Proteins