Unknown

Dataset Information

0

Histone deacetylase 9 (HDAC9) regulates the functions of the ATDC (TRIM29) protein.


ABSTRACT: Histone deacetylase 9 (HDAC9), like most Class II HDACs, catalyzes the removal of acetyl moieties from the ?-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.

SUBMITTER: Yuan Z 

PROVIDER: S-EPMC2998079 | biostudies-literature | 2010 Dec

REPOSITORIES: biostudies-literature

altmetric image

Publications

Histone deacetylase 9 (HDAC9) regulates the functions of the ATDC (TRIM29) protein.

Yuan Zhigang Z   Peng Lirong L   Radhakrishnan Rangasudhagar R   Seto Edward E  

The Journal of biological chemistry 20101014 50


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-pur  ...[more]

Similar Datasets

| S-EPMC2876676 | biostudies-literature
| S-EPMC58507 | biostudies-literature
| S-EPMC4668224 | biostudies-literature
| S-EPMC3961828 | biostudies-literature
| S-EPMC2917523 | biostudies-literature
| S-EPMC5389893 | biostudies-literature
| S-EPMC3091248 | biostudies-literature
| S-EPMC4991412 | biostudies-other
| S-EPMC5451330 | biostudies-literature
| S-EPMC1447420 | biostudies-literature