The Production, Removal and Function of Lysine 2-Hydroxyisobutyrylation Modification
FENG Jin, ZHANG Shuo, WAN Fang*
Khib (lysine 2-hydroxyisobutyrylation), discovered in recent years, is a post-translational modification with distinct structural and functional differences from the well-studied lysine acetylation. Recent mass spectrometry identification and quantification studies have shown that both histone and non-histone proteins can undergo Khib modification. However, there is currently a lack of comprehensive review summarizing the origins and functions of Khib modification. This article summarizes the discovery and sources of Khib, provides a systematic overview of the enzymes involved in the addition and removal of this modification (Writers, Erasers), and highlights proteins affected by Khib modification. The article discusses the relevance of Khib modifications on histone and non-histone proteins to aspects such as gene transcription regulation, protein translation, folding and degradation, influencing cell migration, and regulating metabolic enzyme functions. Additionally, by summarizing the Khib-modified protein sites reported in the literature and conducting motif analysis, a significant motif feature xxKxK is discovered. Pathway enrichment analysis of proteins with Khib modification reported in the literature reveals all aspects of the protein life cycle, including the production of RNA templates, and the translation, localization and degradation of proteins, suggesting that Khib can regulate protein fate. The above analysis and summary not only reveal new functions of Khib but also emphasize the necessity for further in-depth research into the mechanisms of Khib. By exploring the action mechanisms of Khib in different biological processes, a more comprehensive understanding of how this post-translational modification regulates cellular functions and biological processes can be achieved, providing important theoretical foundations and insights for future disease treatments and biological studies.
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