title: Fluorescence anisotropy microplate assay to investigate the interaction of full-length steroid receptor coactivator-1a with steroid receptors.
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).
authors: Department of Biochemistry, University of Illinois at Urbana-Champaign, Urbana, IL, USA.
authors: Chen
authors: C
authors: Zhang
authors: Steven K
authors: SK
authors: Nordeen
authors: David J
authors: DJ
authors: Shapiro
mesh_terms: D000595:Amino Acid Sequence; D001667:Binding, Competitive; D047628:Estrogen Receptor alpha / Q000737:chemistry*; D047629:Estrogen Receptor beta / Q000737:chemistry*; D005454:Fluorescence Polarization / Q000379:methods; D006801:Humans; D007700:Kinetics; D008969:Molecular Sequence Data; D056920:Nuclear Receptor Coactivator 1 / Q000737:chemistry*; D010446:Peptide Fragments / Q000737:chemistry; D011485:Protein Binding; D025941:Protein Interaction Mapping / Q000379:methods*; D020218:Response Elements
chemical_list: C506487:ESR1 protein, human; D047628:Estrogen Receptor alpha; D047629:Estrogen Receptor beta; D010446:Peptide Fragments; C538859:NCOA1 protein, human; D056920:Nuclear Receptor Coactivator 1