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p54nrb acts as a transcriptional coactivator for activation function 1 of the human androgen receptor.

The androgen receptor (AR) has two transactivation functions that have been mapped to the N- and C-terminal domains and designated as activation function-1 (AF-1) and AF-2, respectively. While the molecular basis for AF-2 function has been well studied, little is known about AF-1 coregulators. Therefore, we attempted to identify AF-1-interacting proteins from HEK293 cells by biochemical purification followed by mass fingerprinting by matrix-assisted laser desorption ionization-time-of-flight mass spectrometry (MALDI-TOF MS). Purified AF-1 region-interacting proteins were found to contain nuclear RNA-binding protein p54(nrb), polypyrimidine tract-binding protein-associated splicing factor (PSF), paraspeckle protein 1 (PSP1), and PSP2, which are assumed to be involved in pre-mRNA processing. p54(nrb) interacted with AR via the A/B domain in a ligand-dependent manner. Reflecting the physical interaction between p54(nrb) and the AR A/B domain, AR AF-1 function was potentiated by p54(nrb). Our results suggest that p54(nrb) functions as a coactivator of AR that potentiates transcription, and presumably splicing as well.

Pubmed ID: 12810069

Authors

  • Ishitani K
  • Yoshida T
  • Kitagawa H
  • Ohta H
  • Nozawa S
  • Kato S

Journal

Biochemical and biophysical research communications

Publication Data

July 4, 2003

Associated Grants

None

Mesh Terms

  • Cell Line
  • Genes, Reporter
  • Humans
  • Nuclear Matrix-Associated Proteins
  • Nuclear Proteins
  • Octamer Transcription Factors
  • Peptide Mapping
  • Protein Binding
  • Protein Structure, Tertiary
  • RNA-Binding Proteins
  • Receptors, Androgen
  • Recombinant Fusion Proteins
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
  • Transcriptional Activation