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1. Friedrich Miescher Institute for Biomedical Research, Maulbeerstrasse 66, 4058 Basel, Switzerland 2. Department of Chemistry & Biochemistry, University of Notre Dame, Notre Dame, Indiana 46556, USA email: heinz. gut@ fmi. ch Histone deacetylases (HDACs) form a large family of enzymes catalyzing the removal of ε-N acetyl groups from acetylated lysines on target proteins. HDACs are categorized into four classes with class I, II, and IV containing zinc-dependent enzymes (HDAC 1-11) and class III proteins using nicotine adenine dinucleotide as cofactor (SIRT 1-7)[1]. HDAC6 is a unique class II member as it is the only histone deacetylase featuring two catalytic domains and a C-terminal ubiquitin binding domain. In addition, while most HDACs are located in the nucleus acting on acetylated histone peptides, HDAC6 is mainly found in the cytosol where it regulates acetylation states of a diverse set of proteins …