4 years ago

Beyond histones – the expanding roles of protein lysine methylation

Beyond histones – the expanding roles of protein lysine methylation
Justin Connolly, Zhouran Wu, Kyle K. Biggar
A robust signaling network is essential for cell survival. At the molecular level, this is often mediated by as many as 200 different types of post-translational modifications (PTMs) that are made to proteins. These include well-documented examples such as phosphorylation, ubiquitination, acetylation and methylation. Of these modifications, non-histone protein lysine methylation has only recently emerged as a prevalent modification occurring on numerous proteins, thus extending its role well beyond the histone code. To date, this modification has been found to regulate protein activity, protein–protein interactions and interplay with other PTMs. As a result, lysine methylation is now known to be a coordinator of protein function and is a key driver in several cellular signaling events. Recent advances in mass spectrometry have also allowed the characterization of a growing number of lysine methylation events on an increasing number of proteins. As a result, we are now beginning to recognize lysine methylation as a dynamic event that is involved in a number of biological processes, including DNA damage repair, cell growth, metabolism and signal transduction among others. In light of current research advances, the stage is now set to study the extent of lysine methylation that exists within the entire proteome, its dynamics, and its association with physiological and pathological processes. It is now clear that post-translational lysine methylation extends beyond its well-studied role in the context of histones and chromatin. Research has established that lysine methylation occurs on numerous proteins that regulate diverse cellular pathways and processes with key roles in human health and disease. This review highlights cutting-edge and important findings in the field of non-histone lysine methylation.

Publisher URL: http://onlinelibrary.wiley.com/resolve/doi

DOI: 10.1111/febs.14056

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