The Focal Adhesion Protein Vinexin α Regulates the Phosphorylation and Activity of Estrogen Receptor α

Michel Tujague, Jane S. Thomsen, Kazuhito Mizuki, Christine M. Sadek, Jan Åke Gustafsson

Research output: Contribution to journalArticlepeer-review

19 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)9255-9263
Number of pages9
JournalJournal of Biological Chemistry
Volume279
Issue number10
DOIs
StatePublished - Mar 5 2004

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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