Implications of a polyglutamine tract in the function of the human androgen receptor

Biochem Biophys Res Commun. 2003 Jun 20;306(1):46-52. doi: 10.1016/s0006-291x(03)00902-1.

Abstract

The androgen receptor (AR) is a ligand-dependent transcription factor and belongs to the nuclear receptor family. The AR gene contains a long polymorphic CAG repeat, coding for a polyglutamine tract. In the full size AR, the deletion of the polyglutamine tract results in an increase in the transactivation through canonical AREs. However, this effect is clearly dependent on the response elements, since it is not observed on selective elements. In our assays, a deletion of the repeat positively affected the interactions of the ligand-binding domain with the amino-terminal domain as well as the recruitment of the p160 coactivator SRC-1e to the amino-terminal domain of the AR. This is reflected by an enhanced coactivation of the AR by SRC-1e.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Base Sequence
  • Binding Sites
  • COS Cells
  • Histone Acetyltransferases
  • Humans
  • In Vitro Techniques
  • Nuclear Receptor Coactivator 1
  • Peptides / chemistry*
  • Peptides / genetics
  • Plasmids / genetics
  • Protein Structure, Tertiary
  • Receptors, Androgen / chemistry*
  • Receptors, Androgen / genetics
  • Receptors, Androgen / metabolism*
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • SUMO-1 Protein / metabolism
  • Sequence Deletion
  • Transcription Factors / metabolism
  • Transcriptional Activation

Substances

  • Peptides
  • Receptors, Androgen
  • Recombinant Proteins
  • SUMO-1 Protein
  • Transcription Factors
  • polyglutamine
  • Histone Acetyltransferases
  • NCOA1 protein, human
  • Nuclear Receptor Coactivator 1