Fluorescence anisotropy microplate assay to investigate the interaction of full-length steroid receptor coactivator-1a with steroid receptors

Methods Mol Biol. 2013:977:339-51. doi: 10.1007/978-1-62703-284-1_27.

Abstract

Estrogens, acting via estrogen receptor (ER) play key roles in growth, differentiation, and gene regulation in the reproductive, central nervous, and skeletal systems. ER-mediated gene transcription contributes to the development and spread of breast, uterine, and liver cancer. Steroid receptor coactivator-1a (SRC1a) belongs to the P160 family of coactivators, which is the best known of the many coactivators implicated in ER-mediated transactivation. Binding of full-length P160 coactivators to steroid receptors has been difficult to investigate in vitro. This chapter details how to investigate the interaction of SRC1a with ER using the fluorescence anisotropy/polarization microplate assay (FAMA).

MeSH terms

  • Amino Acid Sequence
  • Binding, Competitive
  • Estrogen Receptor alpha / chemistry*
  • Estrogen Receptor beta / chemistry*
  • Fluorescence Polarization / methods
  • Humans
  • Kinetics
  • Molecular Sequence Data
  • Nuclear Receptor Coactivator 1 / chemistry*
  • Peptide Fragments / chemistry
  • Protein Binding
  • Protein Interaction Mapping / methods*
  • Response Elements*

Substances

  • ESR1 protein, human
  • Estrogen Receptor alpha
  • Estrogen Receptor beta
  • Peptide Fragments
  • NCOA1 protein, human
  • Nuclear Receptor Coactivator 1