| CHD8 belongs to the chromodomain helicase DNA-binding (CHD) family of ATP-dependent chromatin remodeling proteins. The CHD family of proteins has been shown to play an important role in regulating gene expression by utilizing the energy derived from ATP hydrolysis to alter chromatin architecture. The nine CHD family members are characterized by the presence of two tandem chromodomains in the N-terminal region and an SNF2-like ATPase domain near the central region of the protein. In addition, CHD8 contains three CR (conserved region) domains, a SANT (switching-defective protein 3, adaptor 2, nuclear receptor co-repressor, transcription factor IIB)-like domain, two BRK (brahma and kismet) domains, and a DNA-binding domain. The chromatin remodeling activity of CHD8 has been shown to be important for the regulation of a wide variety of genes, such as the HOX genes and genes that are driven by β-catenin, p53, estrogen receptor, or androgen receptor. CHD8 can also interact with the insulator binding protein CTCF and is required for CTCF insulator activity at multiple gene loci. |
