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Vol. 13, Issue 2, 670-682, February 2002
Departments of Microbiology and Urology and The Kaplan
Comprehensive Cancer Center, New York University School of Medicine,
New York, New York 10016
The androgen receptor (AR) is a ligand-regulated transcription
factor that stimulates cell growth and differentiation in
androgen-responsive tissues. The AR N terminus contains two activation
functions (AF-1a and AF-1b) that are necessary for maximal
transcriptional enhancement by the receptor; however, the mechanisms
and components regulating AR transcriptional activation are not fully
understood. We sought to identify novel factors that interact with the
AR N terminus from an androgen-stimulated human prostate cancer cell
library using a yeast two-hybrid approach designed to identify proteins that interact with transcriptional activation domains. A 157-amino acid
protein termed ART-27 was cloned and shown to interact predominantly with the AR153-336, containing AF-1a and a part of AF-1b, localize to the nucleus and increase the transcriptional activity of AR
when overexpressed in cultured mammalian cells. ART-27 also enhanced
the transcriptional activation by AR153-336 fused to the
LexA DNA-binding domain but not other AR N-terminal subdomains, suggesting that ART-27 exerts its effect via an interaction with a
defined region of the AR N terminus. ART-27 interacts with AR in
nuclear extracts from LNCaP cells in a ligand-independent manner. Interestingly, velocity gradient sedimentation of HeLa nuclear extracts
suggests that native ART-27 is part of a multiprotein complex. ART-27
is expressed in a variety of human tissues, including sites of androgen
action such as prostate and skeletal muscle, and is conserved
throughout evolution. Thus, ART-27 is a novel cofactor that interacts
with the AR N terminus and plays a role in facilitating
receptor-induced transcriptional activation.
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