Post-Translational Modification of Proteins in Toxicological Research: Focus on Lysine Acylation.
- Author:
Sangkyu LEE
1
Author Information
1. College of Pharmacy, Research Institute of Pharmaceutical Sciences, Kyungpook National University, Daegu, Korea. sangkyu@knu.ac.kr
- Publication Type:Review
- Keywords:
Lysine acylation;
Post-translational modification;
Toxicoproteomics
- MeSH:
Acetylation;
Acylation;
Aging;
Cell Cycle;
Lysine;
Protein Processing, Post-Translational;
Proteins;
Proteomics;
Toxicology
- From:Toxicological Research
2013;29(2):81-86
- CountryRepublic of Korea
- Language:English
-
Abstract:
Toxicoproteomics integrates the proteomic knowledge into toxicology by enabling protein quantification in biofluids and tissues, thus taking toxicological research to the next level. Post-translational modification (PTM) alters the three-dimensional (3D) structure of proteins by covalently binding small molecules to them and therefore represents a major protein function diversification mechanism. Because of the crucial roles PTM plays in biological systems, the identification of novel PTMs and study of the role of PTMs are gaining much attention in proteomics research. Of the 300 known PTMs, protein acylation, including lysine formylation, acetylation, propionylation, butyrylation, malonylation, succinylation, and crotonylation, regulates the crucial functions of many eukaryotic proteins involved in cellular metabolism, cell cycle, aging, growth, angiogenesis, and cancer. Here, I reviewed recent studies regarding novel types of lysine acylation, their biological functions, and their applicationsin toxicoproteomics research.
