The complete primary structure of human estrogen receptor beta (hER beta) and its heterodimerization with ER alpha in vivo and in vitro

Biochem Biophys Res Commun. 1998 Feb 4;243(1):122-6. doi: 10.1006/bbrc.1997.7893.

Abstract

Human estrogen receptor beta (hER beta) cDNA that encodes the full-length amino acid sequence has been isolated from testis poly(A)+ RNA with the combination of cDNA screening and reverse transcription-PCR. It is composed of a 1590-bp open reading frame and a segment of the 5'- and 3'-untranslated region (UTR) and encodes an additional 53 amino acids in the N-terminal region compared with the previously reported one. Protein interaction between ER alpha and ER beta was demonstrated in vitro by GST pull-down assay and in vivo by immunoprecipitation. Thus, this study indicates that ER alpha and ER beta can interact in vivo, cross-signaling each other.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • COS Cells
  • Cloning, Molecular
  • DNA, Complementary / genetics
  • Dimerization
  • Estrogen Receptor alpha
  • Estrogen Receptor beta
  • Humans
  • In Vitro Techniques
  • Male
  • Molecular Sequence Data
  • Open Reading Frames
  • RNA, Messenger / genetics
  • RNA, Messenger / metabolism
  • Receptors, Estrogen / chemistry*
  • Receptors, Estrogen / genetics*
  • Receptors, Estrogen / metabolism
  • Recombinant Fusion Proteins / chemistry
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / metabolism
  • Testis / metabolism

Substances

  • DNA, Complementary
  • Estrogen Receptor alpha
  • Estrogen Receptor beta
  • RNA, Messenger
  • Receptors, Estrogen
  • Recombinant Fusion Proteins

Associated data

  • GENBANK/AB006590