Chapter 3 - Phosphorylation and Acetylation of Proteins as Posttranslational Modification: Implications in Human Health and Associated Diseases

Abstract

More than 200 posttranslational modifications (PTMs) in proteins have been reported, ranging from different modifications such as phosphorylation acetylation, ubiquitination, SUMOylation, etc. These modifications are observed mostly in eukaryotic proteins, which regulate protein activity and interactions. In order to maintain homeostasis in cells, PTMs in proteins enable cells to respond quickly to various changes. There are numerous changes in properties of proteins such as activity, interaction partners, and sub cellular location. The most extensively studied PTMs are phosphorylation, in which protein kinases attach a phosphate group to serine, threonine, and tyrosine residues, and acetylation wherein an acetyl group is attached to the amino group of amino acids. In fact, Histone acetylation is one of the first PTMs with its role in regulation of chromatin structure. Keeping in view the importance of these two modifications, not only in biological processes but also in health and disease, this chapter has tried to provide an update of these two modifications. Future insights in this direction have also been highlighted.