TY - JOUR
T1 - The Focal Adhesion Protein Vinexin α Regulates the Phosphorylation and Activity of Estrogen Receptor α
AU - Tujague, Michel
AU - Thomsen, Jane S.
AU - Mizuki, Kazuhito
AU - Sadek, Christine M.
AU - Gustafsson, Jan Åke
PY - 2004/3/5
Y1 - 2004/3/5
N2 - 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.
AB - 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.
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U2 - 10.1074/jbc.M312160200
DO - 10.1074/jbc.M312160200
M3 - Article
C2 - 14625289
AN - SCOPUS:1542289886
VL - 279
SP - 9255
EP - 9263
JO - The Journal of biological chemistry
JF - The Journal of biological chemistry
SN - 0021-9258
IS - 10
ER -