Newly Identified Acylation Modifications and Tumor Development
LI Yixiao1,2,3, JIANG Yuhan1,2,3, ZHANG Hongquan1,2,3*
The epigenetic regulation of genes is often jointly determined by the dynamic regulation of chemical groups on histone and non-histone proteins. PTM (post-translational modification), as the main factor of epigenetic regulation, adds small molecules at specific protein sites in the way of covalent linking. Furthermore, it can affect the function, structure, stability and activity of proteins, and finally affect the process of life activities. Miswriting, misreading, or misdeletion of modifying language in chromatin is a common and sometimes early and critical event in human cancer, contributing to tumor development by inducing epigenetic, transcriptome, and phenotypic changes. Lysine, as an amphiphilic amino acid, has hydrophobic side chains and acylation can neutralize the positive charge of lysine, so lysine is the most frequently modified amino acid. Acylation modification can not only change protein structure but also affect protein function. Moreover, it plays a crucial role in DNA transcription, damage repair, oxidative stress, cell metabolism, cell cycle, senescence, angiogenesis and other life activities. Next, this paper reviewed the newly identified acylation modifications recently discovered, and reviewed the discovery, regulation and important role of newly identified acylation modifications in tumor progression in the past decade.
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