Abstract
Acetylation and deacetylation of lysine residues controlled by histone acetyltransferases (HATs) and histone deacetylases (HDACs), respectively, are among the most common posttranslational modifications of proteins. In addition to histones, a large number of nonhistone proteins that can undergo reversible acetylation have been identified. These nonhistone acetylated/deacetylated proteins are involved in a wide range of cellular processes including transcription, translation, DNA repair, metabolism, and cell structure. Aberrant deacetylation of nonhistone proteins is implicated in many human diseases, including cancer. In this chapter, we review and describe the involvement of HDACs in cancer-associated cellular processes via deacetylation of nonhistone proteins, and the possible implications for carcinogenesis and cancer development.
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Acknowledgments
We thank Abuzar Kabir and the Moffitt Proteomics Core for technical help. The work in our lab is supported by grants to E.S. from the National Institutes of Health (NIH), and the Kaul Foundation. L.P. is a recipient of the American Heart Association Postdoctoral Fellowship.
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Peng, L., Seto, E. (2011). Deacetylation of Nonhistone Proteins by HDACs and the Implications in Cancer. In: Yao, TP., Seto, E. (eds) Histone Deacetylases: the Biology and Clinical Implication. Handbook of Experimental Pharmacology, vol 206. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-21631-2_3
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