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- W2970372019 startingPage "453" @default.
- W2970372019 abstract "Histone proteins and their diverse array of post-translational modifications have been subject to exquisite evolutionary conservation in eukaryotes. Accordingly, the factors that control the deposition, removal, and interpretation of histone modifications are themselves deeply conserved, with many strongly impacting development and disease in humans. Of these modifications, lysine methylation has in recent years emerged as a prevalent modification occurring on histone proteins. However, although numerous lysine methyltransferase and demethylase enzymes have been extensively characterized with respect to their ability to control methylation at specific histone residues, their known targets have been rapidly expanding to include the methylation of non-histone proteins as well. These findings extend the role of lysine methylation well-beyond the established histone code and its role in epigenetic regulation. To date, this lysine methylation has been found to directly regulate protein sub-cellular localization, protein-protein interactions, and has also been found to interplay with other post-translational modifications. As a result, lysine methylation is now known to coordinate protein function and be a key driving of a growing list of cellular signaling events, including apoptosis, DNA damage repair, protein translation, cell growth, and signal transduction among others. This chapter will provide insight into the role of protein lysine methylation and its role in regulating protein function and its impact on human development and disease." @default.
- W2970372019 created "2019-09-05" @default.
- W2970372019 creator A5055347268 @default.
- W2970372019 creator A5083508700 @default.
- W2970372019 creator A5089750530 @default.
- W2970372019 date "2019-01-01" @default.
- W2970372019 modified "2023-09-27" @default.
- W2970372019 title "The Role of Protein Lysine Methylation in the Regulation of Protein Function: Looking Beyond the Histone Code" @default.
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