These findings suggest that N-CoR associations with specific corepressor complexes are dynamically regulated and will exhibit promoter and cell-type specificity
2002
Key concepts
Scholarcy highlights
- Members of the nuclear receptor superfamily directly activate or repress target genes by binding to hormone response elements1 in promoter or enhancer regions, and by binding to other DNA sequence-specific activators and can inhibit the transcriptional activities of other classes of transcription factors by transrepression
- Ligand-dependent recruitment of coactivators is dependent on activation function 2, which consists of a short conserved helical sequence within the C terminus of the ligand binding domain
- Biochemical and expression cloning approaches have been used to identify a large number of factors that interact with nuclear receptors in either a ligand-independent or a ligand-dependent manner and are often components of large multiprotein complexes
- As the number of potential coregulators clearly exceeds the capacity for direct interaction by a single receptor, the most plausible hypothesis is that transcriptional activation by nuclear receptors involves the actions of multiple factors
- The yeast SWI1⁄7SNF complex facilitates the binding of sequence-specific transcription factors to nucleosomal DNA and can cause local changes in chromatin structure in an ATP-dependent manner
- A specific conserved corepressor domain of N-CoR and SMRT has been shown to be capable of direct interaction with histone deacetylase 4 and 5. These findings suggest that N-CoR associations with specific corepressor complexes are dynamically regulated and will exhibit promoter and cell-type specificity
- The potential for rapid exchange of nuclear receptors and cofactors has intriguing implications for the functional significance of ever expanding multiple receptors of coregulatory complexes
Need more features? Save interactive summary cards to your Scholarcy Library.