Histone deacetylases (HDACs) are found in large, multisubunit complexes. HDAC1 and HDAC2 are found predominately in either an mSin3A-containing complex or a complex containing the ATP-dependent chromatin remodeling protein, CHD4. The mSin3A complex is recrutied by DNA-binding transcription factors, such as the unligand hormone receptors. In these situations, the HDAC/mSin3A complex is thought to be involved in gene repression. CoREST is a corepressor for REST (RE1 silencing transcription factor) that is found in complex with mSin3A, as well as in non-mSin3A HDAC complexes. CoREST contains an N-terminal and a C-terminal SANT domain, which is common to corepressors involved in steroid horomone receptor gene repression. In non-neuronal cells, CoREST and REST mediate repression of the type II sodium channel promoter. REST is usually found in complex with mSin3A, and under certain conditions may recruit CoREST for repressor activity. The N-terminal SANT domain of CoREST is required for interaction with HDAC1 to form an HDAC complex that does not contain mSin3A or REST. Thus, CoREST is a corepressor that may interact with distinct protein complexes depending on the target for gene repression.
This antibody is routinely tested by western blot analysis. Other applications were tested at BD Biosciences Pharmingen during antibody development only or reported in the literature.