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(Received for publication, July 10, 1997, and in revised form, September 11, 1997)
From the Identical N-terminal deletions in the
wild-type rat androgen receptor (rAR) and a constitutively active rAR
(AR
Volume 272, Number 47,
Issue of November 21, 1997
pp. 29821-29828
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
Interaction between the Amino- and Carboxyl-terminal Regions of
the Rat Androgen Receptor Modulates Transcriptional Activity and Is
Influenced by Nuclear Receptor Coactivators
,
and§
Department of Physiology,
641-902) devoid of the ligand-binding domain (LBD) resulted in
dissimilar consequences in transcriptional activation: deletion of
residues 149-295 abolished wild-type AR activity, but did not
influence that of AR641-902. The activity of the N-terminal
transactivation domain is thus controlled by the hormone-occupied LBD,
suggesting that the N- and C-terminal regions of rAR communicate.
Consistent with this idea, a strong androgen-dependent
interaction between the N-terminal region and LBD was demonstrated in a
mammalian two-hybrid system using GAL4 and VP16 fusion proteins. This
interaction can be direct or indirect. Several nuclear receptor
coactivators (CBP, F-SRC-1, SRC-1, and RIP140) that interact with other
steroid receptors were tested as potential mediators of the N- and
C-terminal interaction of rAR using the mammalian two-hybrid system.
CBP or F-SRC-1 not only enhanced AR-mediated transactivation, but also
facilitated the androgen-dependent interaction between the
N- and C-terminal domains, implying that part of the
coactivator-dependent transcriptional activation
occurs via this mechanism. In contrast, SRC-1, a coactivator for
the progesterone receptor, inhibited both AR-mediated transactivation and interaction between the N and C termini. Recruitment of
coregulators may involve AR domains other than the LBD, as F-SRC-1 and
CBP enhanced, but SRC-1 repressed, the transcriptional activity
of AR641-902. Collectively, interplay between the N-terminal region and LBD of rAR results in the formation of a transactivation complex that includes coregulators and that is mandatory for optimal activation of androgen-induced promoters.
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