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Ligand-Independent Recruitment of SRC-1 to Estrogen Receptor β through Phosphorylation of Activation Function AF-1

Authors
Journal
Molecular Cell
1097-2765
Publisher
Elsevier
Volume
3
Issue
4
Identifiers
DOI: 10.1016/s1097-2765(00)80479-7

Abstract

Abstract The estrogen receptors (ERs) α and β possess a constitutive N-terminal activation function (AF-1) whose activity can be modulated by kinase signaling 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 ERβ in vitro. Enhancement of the interaction between SRC-1 and ERβ AF-1 is also observed in vivo in cells either treated with EGF or expressing activated Ras. Two serine residues in ERβ 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 ERβ via the MAPK pathway.

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