Department of Molecular Oncology, H. Lee Moffitt Cancer Center and Research Institute, Tampa, Florida 33612, USA.
J Biol Chem. 2010 Dec 10;285(50):39329-38. doi: 10.1074/jbc.M110.179333. Epub 2010 Oct 14.
Histone deacetylase 9 (HDAC9), like most Class II HDACs, catalyzes the removal of acetyl moieties from the ε-amino groups of conserved lysine residues in the N-terminal tail of histones. Biologically, HDAC9 regulates a wide variety of normal and abnormal physiological functions, including cardiac growth, T-regulatory cell function, neuronal disorders, muscle differentiation, development, and cancer. In a biochemical approach to identify non-histone substrates of HDAC9, we found that HDAC9 co-purifies specifically with the ataxia telangiectasia group D-complementing (ATDC; also called TRIM29) protein. HDAC9 deacetylates ATDC, alters the ability of ATDC to associate with p53, and consequently inhibits the cell proliferation-promoting activity of ATDC. These results implicate the importance of non-histone deacetylation by HDAC9 and confirm and further extend the multifunctions of this Class II deacetylase.
组蛋白去乙酰化酶 9（HDAC9）与大多数 II 类 HDAC 一样，催化将ε-氨基组上的乙酰基从组蛋白 N 端尾部保守赖氨酸残基上去除。在生物学上，HDAC9 调节广泛的正常和异常生理功能，包括心脏生长、T 调节细胞功能、神经元紊乱、肌肉分化、发育和癌症。在鉴定 HDAC9 的非组蛋白底物的生化方法中，我们发现 HDAC9 与共济失调毛细血管扩张症突变蛋白 D 互补（ATDC；也称为 TRIM29）蛋白特异性共纯化。HDAC9 去乙酰化 ATDC，改变 ATDC 与 p53 结合的能力，从而抑制 ATDC 的促进细胞增殖活性。这些结果表明 HDAC9 的非组蛋白去乙酰化的重要性，并证实和进一步扩展了这种 II 类脱乙酰酶的多功能性。
