Giaimo Benedetto Daniele, Ferrante Francesca, Borggrefe Tilman
Institute of Biochemistry, Justus-Liebig-University Giessen, Friedrichstrasse 24, 35392, Giessen, Germany.
Cell Mol Life Sci. 2024 Dec 16;82(1):5. doi: 10.1007/s00018-024-05531-6.
Post-translational modifications (PTMs) are implicated in many biological processes including receptor activation, signal transduction, transcriptional regulation and protein turnover. Lysine's side chain is particularly notable, as it can undergo methylation, acetylation, SUMOylation and ubiquitination. Methylation affects not only lysine but also arginine residues, both of which are implicated in epigenetic regulation. Beyond histone-tails as substrates, dynamic methylation of transcription factors has been described. The focus of this review is on these non-histone substrates providing a detailed discussion of what is currently known about methylation of hypoxia-inducible factor (HIF), P53, nuclear receptors (NRs) and RELA. The role of methylation in regulating protein stability and function by acting as docking sites for methyl-reader proteins and via their crosstalk with other PTMs is explored.
翻译后修饰（PTMs）参与许多生物学过程，包括受体激活、信号转导、转录调控和蛋白质周转。赖氨酸的侧链尤为显著，因为它可以发生甲基化、乙酰化、SUMO化和泛素化。甲基化不仅影响赖氨酸，还影响精氨酸残基，这两种残基都参与表观遗传调控。除了组蛋白尾巴作为底物外，还描述了转录因子的动态甲基化。本综述的重点是这些非组蛋白底物，详细讨论了目前关于缺氧诱导因子（HIF）、P53、核受体（NRs）和RELA甲基化的已知情况。探讨了甲基化通过作为甲基阅读蛋白的对接位点以及通过与其他PTMs的相互作用来调节蛋白质稳定性和功能的作用。
