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, 3 (4), 513-9

Ligand-independent Recruitment of SRC-1 to Estrogen Receptor Beta Through Phosphorylation of Activation Function AF-1

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Ligand-independent Recruitment of SRC-1 to Estrogen Receptor Beta Through Phosphorylation of Activation Function AF-1

A Tremblay et al. Mol Cell.

Abstract

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.

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