| First Author | Tremblay A | Year | 1999 |
| Journal | Mol Cell | Volume | 3 |
| Issue | 4 | Pages | 513-9 |
| PubMed ID | 10230404 | Mgi Jnum | J:54901 |
| Mgi Id | MGI:1336576 | Doi | 10.1016/s1097-2765(00)80479-7 |
| Citation | Tremblay A, et al. (1999) Ligand-independent recruitment of SRC-1 to estrogen receptor beta through phosphorylation of activation function AF-1. Mol Cell 3(4):513-9 |
| abstractText | The estrogen receptors (ERs) alpha and beta possess a constitutive N- terminal activation function (AF-1) whose activity can be modulated by kinase signalling pathways. We demonstrate here that phosphorylation of AF-1 by MAP kinase (MAPK) leads to the recruitment of steroid receptor coactivator-1 (SRC-1) by ER beta in vitro. Enhancement of the interaction between SRC-1 and ER beta AF-1 is also observed in vivo in cells either treated with EGF or expressing activated Ras. Two serine residues in ER beta AF-1, of which one is contained within a motif present in other steroid receptors, are critical for physical interaction with SRC-1 and transcriptional activation. Our results establish a role for nuclear receptor phosphorylation in the recruitment of SRC-1 and provide a molecular basis for ligand- independent activation by ER beta via the MAPK pathway. |
