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Example sentences for: src-
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To test the effects of rexinoids on coactivator binding in a defined biochemical system, surface plasmon resonance was used to characterize the effects of the various ligands on binding of CAR, RXR and CAR/RXR heterodimers to SRC-3 (also known as ACTR, p/CIP, RAC3, AIB1, TRAM-1), an effective coactivator for CAR and many other members of the nuclear receptor superfamily.
Here, we describe the effect of coactivator proteins SRC-1 (Acc# AJ000882, U90661, Table 1) and p300 (Acc# U01877, Table 3), and their relation to differentiation genes such as retinoic acid receptor (RAR/PML, Acc#: X06614, Table 1), and Leptin receptor variant (Acc#: U66496, Table 1); all of which are down-regulated in Tat expressing cells (Figure 5).
Overexpression of these NCoA factors enhances ligand-induced transactivation of several nuclear receptors [ 99 ] . A weak intrinsic HAT activity has been reported in SRC-1/NCoA-1 and pCIP/ACTR/AIB1, suggesting that chromatin remodeling may also be a function of these NCoA factors [ 99 100 ] ; although they do not appear to contain regions homologous to the HAT domains of CBP/p300 or p/CAF.
The effect of ligands on coactivator binding was evaluated using the BIAcore instrument as described [ 25 26 ] . For interaction of CAR, RXR and CAR/RXR heterodimer with SRC-3, a GST-SRC-3 fusion protein containing the receptor interaction domain of the coactivator was expressed in bacteria and purified.
The nuclear receptor (NR) family comprises 48 structurally related transcription factors, many of which require their cognate ligand for activity [ 1 2 3 ] . The NRs regulate transcription by binding to response elements in the promoters of target genes and acting as scaffolds for the assembly of large coactivator and corepressor complexes [ 4 ] . NR coactivators include the p160s (including GRIP1/TIF-2, SRC-1 and AIB1/ACTR/pCIP).
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