Abstract
Oncogenesis is a multistep process mediated by a variety of factors including epigenetic modifications. Global epigenetic post-translational modifications have been detected in almost all cancers types. Epigenetic changes appear briefly and do not involve permanent changes to the primary DNA sequence. These epigenetic modifications occur in key oncogenes, tumor suppressor genes, and transcription factors, leading to cancer initiation and progression. The most commonly observed epigenetic changes include DNA methylation, histone lysine methylation and demethylation, histone lysine acetylation and deacetylation. However, there are several other novel post-translational modifications that have been observed in recent times such as neddylation, sumoylation, glycosylation, phosphorylation, poly-ADP ribosylation, ubiquitination as well as transcriptional regulation and these have been briefly discussed in this article. We have also highlighted the diverse epigenetic changes that occur during the process of tumorigenesis and described the role of histone modifications that can occur on tumor suppressor genes as well as oncogenes, which regulate tumorigenesis and can thus form the basis of novel strategies for cancer therapy.
Highlights
Post translational modifications (PTMs) on histone as well as non-histone proteins regulate gene expression profiles through chromatin structure alterations
This study indicated the early reduction of OGlcNAcylation level at H3 on serine 10 and 28 in S phase whereas elevated levels was observed in G2/M phase
PTMs of histones such as histone acetyltransferases and deacetylases have been identified in the initiation, progression, and metastasis of cancers and some of these events are indicators of poor prognosis
Summary
Post translational modifications (PTMs) on histone as well as non-histone proteins regulate gene expression profiles through chromatin structure alterations. PTMs such as phosphorylation, N-terminal acetylation, methylation, sumoylation, ubiquitination, propionylation, butyrylation, carbonylation, neddylation, proline isomerization, glycosylation, citrullination and poly ADP ribosylation regulate diverse protein functions [1, 2]. It has been shown that PC4 interaction with p53 leads to acetylation of both the proteins and enhances the p53 DNA binding ability and expresses p53 regulated gene products, especially during DNA damage [41, 42].
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