Abstract：
:Post-translational acetylation of lysines is most extensively studied in histones, but this modification is also found in many other proteins and is implicated in a wide range of biological processes in both the cell nucleus and the cytoplasm. Like phosphorylation, acetylation patterns and levels are often altered in cancer, therefore small molecule inhibition of enzymes that regulate acetylation and deacetylation offers much potential for inhibiting cancer cell growth, as does disruption of interactions between acetylated residues and 'reader' proteins. For more than a decade now, histone deacetylase inhibitors have been investigated for their ability to increase acetylation and promote expression of tumor suppressor genes. However, emerging evidence suggests that acetylation can also promote cancer, in part by enhancing the functions of oncogenic transcription factors. In this review, we focus on how acetylation of both histone and non-histone proteins may drive cancer, and we will discuss the implications of such changes on how patients are assigned to therapeutic agents. Finally, we will explore what the future holds in the design of small-molecule inhibitors for modulation of levels or functions of acetylation states.
journal_name
Oncogenejournal_title
Oncogeneauthors
Farria A,Li W,Dent SYdoi
10.1038/onc.2014.453subject
Has Abstractpub_date
2015-09-17 00:00:00pages
4901-13issue
38eissn
0950-9232issn
1476-5594pii
onc2014453journal_volume
34pub_type
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