RSRC1 SUMOylation enhances SUMOylation and inhibits transcriptional activity of estrogen receptor β

FEBS Lett. 2015 Jun 4;589(13):1476-84. doi: 10.1016/j.febslet.2015.04.035. Epub 2015 Apr 30.

Abstract

The transcription factor estrogen receptor β (ERβ) plays roles in the central nervous, endocrine, cardiovascular, and immune systems. ERβ can be SUMOylated. However, the underlying mechanism remains unclear. Here, we show that RSRC1/SRrp53 interacts with ERβ and SUMOylation of RSRC1 is required for regulation of PIAS1-mediated ERβ SUMOylation. RSRC1 promotes ERβ SUMOylation through enhanced interaction between ERβ and PIAS1. RSRC1 represses ERβ transcriptional activity through regulation of ERβ SUMOylation. By establishing RSRC1 as a novel cofactor for SUMOylation, our data provide insight into regulation of ERβ SUMOylation and indicate that SUMOylation of one protein can regulate another protein SUMOylation.

Keywords: ERβ; PIAS1; RSRC1/SRrp53; SUMOylation; Transcriptional activity.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Line, Tumor
  • Estrogen Receptor beta / genetics
  • Estrogen Receptor beta / metabolism*
  • HEK293 Cells
  • Humans
  • Immunoblotting
  • Nuclear Proteins / genetics
  • Nuclear Proteins / metabolism*
  • Protein Binding
  • Protein Inhibitors of Activated STAT / genetics
  • Protein Inhibitors of Activated STAT / metabolism
  • Protein Interaction Mapping
  • Sumoylation*
  • Transcription, Genetic*
  • Two-Hybrid System Techniques

Substances

  • Estrogen Receptor beta
  • Nuclear Proteins
  • Protein Inhibitors of Activated STAT
  • RSRC1 protein, human