Mechanisms of Signal Transduction
The Focal Adhesion Protein Vinexin α Regulates the Phosphorylation and Activity of Estrogen Receptor α*

https://doi.org/10.1074/jbc.M312160200Get rights and content
Under a Creative Commons license
open access

Steroid receptors are transcription factors that regulate hormone-responsive genes and whose activity is controlled by their interaction with numerous other proteins. Observations reported here reveal that estrogen receptors α and β (ERα and ERβ), androgen receptor, and glucocorticoid receptor bind in vitro to vinexin α, a multiple SH3 motif-containing protein associated with the cytoskeleton. The SH3 domains are not involved in this interaction. Furthermore, we demonstrate that vinexin α stimulates the ligand-induced transactivation function of these receptors, although it is devoid of intrinsic transcriptional activity when tethered to DNA. In addition, the ectopic coexpression of vinexin α and ERα results in a loss of ERα phosphorylation on serines and the partial redistribution of vinexin α into the nucleus, where it colocalizes with ERα. These results establish a new model of transcriptional regulation where components of the cell-cell and cell-substrate adhesion complexes can regulate the phosphorylation and activity of steroid receptors.

Cited by (0)

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank/EBI Data Bank with accession number(s) AF439378.

*

This work was supported by the Swedish Cancer Fund and KaroBio AB. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked “advertisement” in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.