Abstract
Alzheimer's disease (AD) is one of the most common neurodegenerative diseases and a major cause of death among elderly individuals. The etiology of AD involves a combination of genetic, environmental, and lifestyle factors. A number of epigenetic alterations in AD have recently been reported; for example, studies have found an increase in histone acetylation in patients with AD and the protective function of histone deacetylase inhibitors. The histone acetylases in the MYST family are involved in a number of key nuclear processes, such as gene-specific transcriptional regulation, DNA replication, and DNA damage response. Therefore, it is not surprising that they contribute to epigenetic regulation as an intermediary between genetic and environmental factors. MYST proteins also exert acetylation activity on non-histone proteins that are closely associated with the pathogenesis of AD. In this review, we summarized the current understanding of the roles of MYST acetyltransferases in physiological functions and pathological processes related to AD. Additionally, using published RNA-seq, ChIP-seq, and ChIP-chip data, we identified enriched pathways to further evaluate the correlation between MYST and AD. The recent research described in this review supports the importance of epigenetic modifications and the MYST family in AD, providing a basis for future functional studies.
Highlights
Alzheimer's disease (AD) is one of the most common neurodegenerative diseases and a major cause of death among elderly individuals
Since the year 2000, the mortality rate for AD has increased by 89% while that for heart diseases has decreased by 14% during the same period
It is estimated that the total medical investment in AD may reach 1.1 trillion dollars by the year 2050 in the United States alone [1]
Summary
One of the main types of histone modification, involves the addition of an acetyl group to lysine residues in the N-terminal tail or on the surface of the nucleosome core of histones. The MYST family currently includes five human HATs, Tip, MOZ, MORF, HBO1, and MOF, and orthologs have been detected in other eukaryotes They function in multi-subunit protein complexes with evolutionarily conserved compositions. MOF (males absent on the first) usually functions as a catalytic subunit in acetyltransferase complexes In human cells, it can form two different protein complexes (MSL and NSL), both of which acetylate histone H4 at lysine 16 (H4K16). To establish the direct link between MOF and AD, we performed an additional PANTHER pathway analysis based on ChIP-seq data for MOF-binding motifs in the embryonic stem cells [64] (Figure 7A) and PANTHER pathway analyses of the genes that were significantly altered in the MOF-deleted mouse embryonic fibroblasts [63] (Figure 7B). Various genes associated with the pathogenesis of AD as well as the AD-related cellular processes were identified
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