Nuclear receptor coactivator 1 (NCOA1, also known as SRC-1) belongs to the SRC/p160 nuclear receptor coactivator family, which contains proteins that are ligand-dependent transcription factors []. These receptors can function as molecular switches [].NCOA1 directly binds nuclear receptors and stimulates the transcriptional activities in a hormone-dependent fashion []. It is involved in the coactivation of different nuclear receptors, such as for steroids (PGR, GR and ER), retinoids (RXRs), thyroid hormone (TRs) and prostanoids (PPARs) []. It is also involved in coactivation mediated by STAT3, STAT5A, STAT5B and STAT6 transcription factors [, , ]. It plays a central role in creating multisubunit coactivator complexes that act via remodeling of chromatin, and possibly acts by participating in both chromatin remodeling and recruitment of general transcription factors []. It can be regulated by sumoylation and ubiquitination [].
This family represents the C terminus of mammalian STAT6 (signal transducer and activator of transcription 6). It contains an LXXLL motif which binds to NCOA1 (Nuclear receptor coactivator 1) [].
This entry represents the interlocking domain of the eukaryotic nuclear receptor coactivators Ncoa1, Ncoa2 and Ncoa3. The interlocking domain forms a 3-helical non-globular array that forms interlocked heterodimers with its target.Nuclear receptors are ligand-activated transcription factors involved in the regulation of many processes, including development, reproduction and homeostasis. Nuclear receptor coactivators act to modulate the function of nuclear receptors. Coactivators associate with promoters and enhancers primarily through protein-protein contacts to facilitate the interaction between DNA-bound transcription factors and the transcription machinery. In addition to their role as coactivators of various nuclear receptors, Ncoa1 and Ncoa3 both have histone acetyltransferase activity (), but Ncoa2 does not [, ].
This entry represents the interlockingdomain superfamily of the eukaryotic nuclear receptor coactivators Ncoa1, Ncoa2 and Ncoa3. The interlocking domain forms a 3-helical non-globular array that forms interlocked heterodimers with its target.Nuclear receptors are ligand-activated transcription factors involved in the regulation of many processes, including development, reproduction and homeostasis. Nuclear receptor coactivators act to modulate the function of nuclear receptors. Coactivators associate with promoters and enhancers primarily through protein-protein contacts to facilitate the interaction between DNA-bound transcription factors and the transcription machinery. In addition to their role as coactivators of various nuclear receptors, Ncoa1 and Ncoa3 both have histone acetyltransferase activity (), but Ncoa2 does not [, ].
This superfamily represents the interlocking domain of various eukaryotic nuclear receptor coactivators, including CREBP, P300, Ncoa1, Ncoa2 and Ncoa3. The interlocking domain forms a 3-helical non-globular array that forms interlocked heterodimers with its target.Nuclear receptors are ligand-activated transcription factors involved in the regulation of many processes, including development, reproduction and homeostasis. Nuclear receptor coactivators act to modulate the function of nuclear receptors. Coactivators associate with promoters and enhancers primarily through protein-protein contacts to facilitate the interaction between DNA-bound transcription factors and the transcription machinery. Many of these coactivators are structurally related, including CBP (CREB-binding protein), P300 and ACTR (activator for thyroid and retinoid receptors) []. CBP and P300 both have histone acetyltransferase activity (). CBP/P300 proteins function synergistically to activate transcription, acting to remodel chromatin and to recruit RNA polymerase II and the basal transcription machinery. CBP is required for proper cell cycle control, differentiation and apoptosis. The interaction of CBP/P300 with transcription factors involves several small domains. The IBiD domain in the C-terminal of CBP is responsible for CBP interaction with IRF-3, as well as with the adenoviral oncoprotein E1A, TIF-2 coactivator, and the IRF homologue KSHV IRF-1 [].Ncoa1, Ncoa2 and Ncoa3 are all coactivators of various nuclear receptors. In addition, Ncoa1 and Ncoa3 both have histone acetyltransferase activity, but Ncoa2 does not [, ].
