Cyclin D1 Binds the Androgen Receptor and Regulates Hormone-Dependent Signaling in a p300/CBP-Associated Factor (P/CAF)-Dependent Manner

The androgen receptor (AR) is a ligand-regulated member of the nuclear receptor superfamily. The cyclin D1 gene product, which encodes the regulatory subunit of holoenzymes that phosphorylate the retinoblastoma protein (pRB), promotes cellular proliferation and inhibits cellular differentiation in s...

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Published in:Molecular endocrinology (Baltimore, Md.) Md.), 2001-05, Vol.15 (5), p.797-811
Main Authors: Reutens, Anne T, Fu, Maofu, Wang, Chenguang, Albanese, Chris, McPhaul, Michael J, Sun, Zijie, Balk, Steven P, Jänne, Olli A, Palvimo, Jorma J, Pestell, Richard G
Format: Article
Language:English
Subjects:
Acetyltransferases - antagonists & inhibitors
Acetyltransferases - metabolism
Acetyltransferases - physiology
Amino Acid Sequence
Androgen Receptor Antagonists
Blotting, Western
Cell Cycle Proteins - antagonists & inhibitors
Cell Cycle Proteins - metabolism
Cell Cycle Proteins - physiology
Cyclin D1 - metabolism
Cyclin D1 - physiology
Histone Acetyltransferases
Humans
Ligands
Male
Molecular Sequence Data
Mutation
p300-CBP Transcription Factors
Prostatic Neoplasms - metabolism
Receptors, Androgen - metabolism
Receptors, Androgen - physiology
Sequence Alignment
Signal Transduction - physiology
Transcription Factors
Tumor Cells, Cultured
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Summary:The androgen receptor (AR) is a ligand-regulated member of the nuclear receptor superfamily. The cyclin D1 gene product, which encodes the regulatory subunit of holoenzymes that phosphorylate the retinoblastoma protein (pRB), promotes cellular proliferation and inhibits cellular differentiation in several different cell types. Herein the cyclin D1 gene product inhibited ligand-induced AR- enhancer function through a pRB-independent mechanism requiring the cyclin D1 carboxyl terminus. The histone acetyltransferase activity of P/CAF (p300/CBP associated factor) rescued cyclin D1-mediated AR trans-repression. Cyclin D1 and the AR both bound to similar domains of P/CAF, and cyclin D1 displaced binding of the AR to P/CAF in vitro. These studies suggest cyclin D1 binding to the AR may repress ligand-dependent AR activity by directly competing for P/CAF binding.
ISSN:0888-8809
1944-9917
DOI:10.1210/mend.15.5.0641