Deacetylation of Nonhistone Proteins by HDACs and the Implications in Cancer

Lirong Peng and Edward Seto

Contents

1 Introduction 40

2 HDACs and Apoptosis 42

3 HDACs and Autophagy 43

4 HDACs and DNA Damage Repair/Genome Integrity 44

5 HDACs and Differentiation 45

6 HDACs and Invasion/Metastasis 47

7 HDACs and Tumor Immune Responses 48

8 HDACs and Viral Proteins 48

9 Discussion and Perspective 49

References 50

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 acety-lation 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.

Keywords HDAC • Histone deacetylase • Nonhistone acetylation • Nonhistone deacetylation • Cancer

H. Lee Moffitt Cancer Center & Research Institute, Department of Molecular Oncology, 12902 Magnolia Drive, Tampa, Florida 33612, USA e-mail: [email protected]

T.-P. Yao and E. Seto (eds.), Histone Deacetylases: the Biology and Clinical Implication, 39 Handbook of Experimental Pharmacology 206, DOI 10.1007/978-3-642-21631-2_3, © Springer-Verlag Berlin Heidelberg 2011

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