NCOA1

(redirected from SRC-1)

NCOA1

A gene on chromosome 2p23 that encodes a protein of the p160/steroid receptor coactivator family, which acts as a transcriptional coactivator for steroid and nuclear hormone receptors, coactivating different nuclear receptors—e.g., 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, and may participate in chromatin remodelling and recruitment of general transcription factors. NCOA1 acts with NCOA2 to control energy balance between white and brown adipose tissues.
References in periodicals archive ?
First, we assayed chemicals to determine their ability to modulate direct interaction between the hER[Alpha] and the steroid receptor coactivator-1 (SRC-1) and in a competition binding assay to displace 17[Beta]-estradiol ([E.sub.2]).
This assay is based on the direct ligand-dependent interaction between the ER and the transcriptional steroid receptor coactivator-1 (SRC-1) after activation of the receptor, which results from a ligand-induced conformational change.
In the CARLA test, none of the xenobiotics studied was able to induce interaction between ER and SRC-1; this is similar to results with the antiestrogens ICI 182,780 and hydroxytamoxifen.
The pGEX GST-hER and pSG5 SRC-1 plasmids (34) were a gift from M.
Beads were incubated with the test compounds ([E.sub.2], DES, xenobiotic) and radiolabeled SRC-1 (produced in vitro using a coupled transcription/translation rabbit reticulocyte lysate system (TNT; Promega, Madison, WI).
This assay is based on the ligand-induced binding of SRC-1 to nuclear hormone receptors (34).
SRC-1 was expressed and labeled with [[sup.35]S]-methionine, and the LBD of ER was expressed in Escherichia coli as a fusion protein with glutathione-S-transferase (GST).
This property was used in the CARLA to identify potential ER ligands with a specific interaction between the coactivator SRC-1 and the fusion protein GST-ER[Alpha] LBD.
Our results demonstrate that, in contrast to [E.sub.2], none of the environmental pollutants tested was able to induce an interaction between SRC-1 and the ER[Alpha] LBD.