Post-translational modification of proteins in toxicological research: focus on lysine acylation.
Post-translational modification of proteins in toxicological research: focus on lysine acylation.
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DOI：
10.5487/tr.2013.29.2.081
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发表时间：
2013-06
影响因子：
2.3
通讯作者：
Lee S
中科院分区：
文献类型：
--
作者：
Lee S
Toxicoproteomics将蛋白质组学知识整合到毒理学中，使生物液体和组织中的蛋白质定量，从而将毒理学研究提升到一个新的水平。翻译后修饰（PTM）通过共价结合小分子来改变蛋白质的三维（3D）结构，因此代表了主要的蛋白质功能多样化机制。由于PTM在生物系统中的重要作用，新的PTM的鉴定和研究PTM的作用在蛋白质组学研究中越来越受到关注。在300种已知的PTM中，蛋白质酰化，包括赖氨酸酰化、乙酰化、丙酰化、丁酰化、丙二酰化、琥珀酰化和巴豆酰化，调节参与细胞代谢、细胞周期、衰老、生长、血管生成和癌症的许多真核蛋白质的关键功能。本文就赖氨酸酰化的新类型、其生物学功能及其在毒物蛋白质组学研究中的应用作一综述。
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.