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Department of Cell Biology, Baylor College of Medicine, Houston, Texas 77030
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ABSTRACT |
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 TOP ABSTRACT INTRODUCTIONRESULTSDISCUSSIONMATERIALS AND METHODSREFERENCES |
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35,
which lacks the repressor domain (the C-terminal 35 amino acids), fails
to relieve this repression. This finding suggests that the repressor
domain of COUP-TFI may squelch a limiting amount of corepressor in HeLa
cells. In addition, increasing concentrations of TRß also can relieve
the COUP-TFI repression in a hormone-sensitive manner. Similarly,
overexpression of increasing concentration of COUP-TFI, but not
COUP-TFI35, can squelch the silencing activity of the unliganded
TRß. Collectively, these results indicate that COUP-TFI and TRß
share a common corepressor(s) for their silencing activity. To
determine which corepressor is involved in the COUP-TF-silencing
activity, we used a yeast two-hybrid and in vitro GST
pull-down assays to demonstrate that COUP-TFI can interact with the
fragment of N-CoR (nuclear receptor-corepressor) encoding amino acids
921-2453 and the fragments of SMRT (silencing mediator for retinoic
acid receptor and TR) encoding amino acids 29–564 and 565-1289,
respectively. Interestingly, the fragment of SMRT encoding amino acids
1192–1495, which strongly interacts with TRß, interacts very weakly
with COUP-TFI. Furthermore, overexpression of N-CoR or SMRT potentiates
the silencing activity of COUP-TFI and can relieve the
COUP-TFI-mediated squelching of Gal4-COUP-TFI activity. Therefore, our
studies indicate that N-CoR and SMRT act as corepressors for the
COUP-TFI silencing activity. |
INTRODUCTION |
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TOPABSTRACTINTRODUCTIONRESULTSDISCUSSIONMATERIALS AND METHODSREFERENCES |
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Silencing activity of unliganded TR and RAR requires limiting factors termed corepressors (5). Recently, two corepressors that bind to unliganded TR and RAR have been cloned using a yeast two-hybrid screen: N-CoR (nuclear receptor-corepressor) (10, 11) and SMRT (silencing mediator for RAR and TR) (12, 13, 14, 15). Binding of these corepressors is necessary for unliganded receptors to silence the activity of target promoters. Prevailing evidence suggests that binding of hormone changes the conformation of the receptors, which results in the release of the corepressor and recruitment of coactivators, thereby abolishing their silencing activity. These two corepressors exhibit significant sequence homologies in their receptor-interacting domains, suggesting the existence of a corepressor gene family. COUP-TFs (chicken ovalbumin upstream promoter-transcription factors) belong to the steroid receptor superfamily and are classified as orphan receptors because their ligand has yet to be defined. There are two COUP-TF genes in mammals, COUP-TFI and COUP-TFII. COUP-TFs have been implicated in neurogenesis, organogenesis, and cell fate determination (16, 17, 18, 19). COUP-TFs can form stable homodimers and bind to a variety of hormone response elements recognized by other members of the steroid receptor superfamily, such as RAR, retinoid X receptor (RXR), TR, vitamin D receptor (VDR), peroxisome proliferator-activated receptor, and hepatocyte nuclear factor 4. COUP-TFs can thereby inhibit transcriptional activities of these receptors on both consensus and natural response elements (17, 20). Four mechanisms have been proposed to address COUP-TF’s ability to inhibit the transactivation function of other members of the steroid receptor superfamily. First, COUP-TFs repress the hormone-dependent transactivation of target genes by VDR, TR, and RAR through direct competition for occupancy of their response elements (21, 22, 23). Second, COUP-TFs heterodimerize with RXR to reduce the available concentration of RXR for heterodimerization with TR, VDR, RAR, and peroxisome proliferator-activated receptor and thus indirectly interfere with these receptors to transactivate their target genes (21, 22, 24, 25, 26, 27). Third, COUP-TFs can tether to DNA via LBD-LBD interactions with TR, RAR, and RXR to transrepress their activities (27). Finally, COUP-TFs have been shown to repress basal and activator-dependent transcriptional activities of various promoters when their binding site is placed upstream or downstream of these promoters (27). The silencing domain in COUP-TFs was localized to the C terminus of the putative LBD, which can be transferred to the heterologous Gal4 DNA-binding domain (DBD). Activators that can be repressed by COUP-TFs include acidic (Gal4-RII), glutamine-rich (Gal4-ftzQ), proline-rich (Gal4-CTF1P), and Ser/Thr-rich (Gal4-ZenST) transactivators (27). Because COUP-TF can repress such a diverse group of transactivators, it is unlikely that COUP-TF’s repression is through direct quenching of these transactivators or by interfering with their respective targets. It is rather likely that COUP-TFs interact with a common target, a putative corepressor(s) that mediates their repression.
To substantiate this hypothesis, we address two major questions in this paper; 1) Does COUP-TFI-mediated repression require corepressors? and 2) If it does, does COUP-TFI share corepressors with other receptors, such as TR and RAR? To answer these questions, we first examined whether cofactors are involved in COUP-TFI-mediated repression using either self-squelching or TR/COUP-TF-mediated mutual squelching experiments. Next, we examined whether COUP-TFI can interact with N-CoR or SMRT. Finally, we examined whether N-CoR or SMRT can function as a corepressor in COUP-TFI-mediated repression. Results from these experiments indicate that both N-CoR and SMRT can function as corepressors for COUP-TFI-mediated repression of target genes.
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RESULTS |
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TOPABSTRACTINTRODUCTIONRESULTSDISCUSSIONMATERIALS AND METHODSREFERENCES |
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). This repression activity can be
reversed by the exogenously expressed LBD of COUP-TFI (184–423), which
does not bind to the reporter construct, in a dose-dependent manner.
The observed release of repression cannot be attributed to the
nonspecific effect of overexpression of COUP-TFI on Gal DNA-binding
activity because overexpression of COUP-TFI had little effect on the
basal promoter activity when cotransfected with the Gal4 DBD alone
(27). In contrast, COUP-TFI mutant, COUP-TFI35 (amino acid
184–388), which does not contain a repressor domain, cannot reverse
Gal4-COUP-TFI-mediated repression. Overexpression of COUP-TFI or
COUP-TFI35 does not affect the basal promoter activity of Gal4 (data
not shown). These results clearly indicate that a limiting factor,
termed corepressor(s), is required for the activity of
COUP-TFI-mediated repression. These results also suggest that the
C-terminal 35 amino acids are required for interaction with the
putative corepressor(s).
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). Similarly,
overexpression of TR mutant, TR168–456(V174A/D177A), which loses its
silencing activity but retains hormone-dependent transactivation (28),
cannot relieve the basal repression activity of Gal4-COUP-TFI (lines
9–11, Fig. 2). These findings strongly suggest that TRß- and
COUP-TFI-mediated repression share the same corepressor(s).
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, transfection of Gal4-TRß into HeLa cells significantly repressed the
basal promoter activity of the reporter construct. Overexpression of
COUP-TFI can reverse this repression in a dose-dependent manner. As
expected, we observe no reversal of TRß-mediated repression by
overexpression of the repression-defective COUP-TFI mutant,
COUP-TFI35. These results further suggest that common corepressors
are shared by COUP-TFI and TRß for their repression activity.
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, A and B, a
fragment of N-CoR encoding amino acids 921-2453 and fragments of SMRT
encoding amino acids 565-1495 and 1192–1495 can interact with TRß in
a hormone-dependent manner as previously described (10, 12, 14). It
should be pointed out that, to our surprise, a larger fragment of N-CoR
encoding amino acids 190-2453, which contains a fragment of N-CoR
encoding amino acids 921-2453, cannot interact with TRß in a yeast
two-hybrid assay. Although the reason for this discrepancy is not clear
at present, it is possible that the N-terminal repression domain of
N-CoR encoding amino acids 190–920 is very potent and overrides the
activation function of Gal4 in a yeast two-hybrid assay. This notion is
further supported by our observation that a fragment of N-CoR encoding
amino acids 190-2453 can interact with TRß in vitro (data
not shown).
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). In
contrast, as a positive control, we showed a strong interaction between
Gal4•DBD-COUP-TFI and Gal4•AD-TFIIB (lane 7 in Fig. 4C). We then
examined the interaction of various deletion fragments of N-CoR or SMRT
with COUP-TFI (Fig. 4C). In a yeast two-hybrid assay system, the
interaction of COUP-TFI with N-CoR or SMRT was detected when COUP-TFI
was bound to DNA response element. In the absence of DNA response
element, no interaction was observed (data not shown). A fragment of
N-CoR encoding amino acids 921-2453 strongly interacts with COUP-TFI;
however, a fragment of N-CoR encoding amino acids 190-2453 does not
interact with COUP-TFI in a yeast two-hybrid assay. Similar to the
TRß interaction study (Fig. 4B), the repression domains of N-CoR
encoding amino acids 190–920 may interfere with the Gal4 activation
domain function in a yeast two-hybrid assay; thus, a fragment of N-CoR
encoding amino acids 190-2453 is not able to activate ß-galactosidase
activity of the reporter. However, both N-CoR fragments encoding amino
acids 190-2453 and 921-2453 were found to interact with COUP-TFI in an
in vitro glutathione S-transferase (GST)
pull-down assay because these in vitro interactions are
presumably not influenced by the repressor function of N-CoR. Thus, a
fragment of COUP-TFI encoding amino acids 56–423 can interact
specifically with N-CoR in yeast and in vitro. On the other
hand, fragments of SMRT encoding amino acids 29–564 and 565-1495
strongly interact with COUP-TFI (Fig. 4C). In contrast, a fragment of
SMRT encoding amino acids 1192–1495, which interacts well with TR,
interacts only weakly with COUP-TFI in a yeast two-hybrid assay (Fig. 4C). These results suggest that the COUP-TFI-interacting domain of SMRT
is located mainly at amino acids 29–564 and 565-1191. These
interaction data in yeast are further supported by the in
vitro protein-protein interactions as shown in Fig. 5B. Both fragments of SMRT encoding amino acids 29–564
and 565-1289 are able to interact with GST-COUP-TFI, whereas a fragment
of SMRT encoding amino acids 1192–1495 fails to interact with
GST-COUP-TFI.
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, neither N-CoR nor
SMRT have a significant effect on transcription activity of the
reporter construct in the absence of cotransfected Gal4-COUP-TFI.
However, both N-CoR and SMRT can potentiate the repressor function of
Gal4-COUP-TFI in a dose-dependent manner in HeLa cells. These data
suggest that both N-CoR and SMRT can function as corepressors of
COUP-TFI in HeLa cells. Thus, it is likely that they are the endogenous
corepressors of COUP-TFI in HeLa cells.
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), overexpression of COUP-TFI can squelch
the repressor activity of Gal4-COUP-TFI. If N-CoR and SMRT are the
limiting factors required for COUP-TFI-mediated repression, we expect
that overexpression of N-CoR or SMRT should reverse this squelching
activity. As shown in Fig. 7, overexpression of N-CoR or
SMRT was able to relieve the squelching effects of COUP-TFI on
Gal4-COUP-TFI repression function in a dose-dependent manner. On the
other hand, overexpression of N-CoR or SMRT had no significant effect
on transcription activity of the reporter construct in the absence of
cotransfected Gal4-COUP-TFI (data not shown). Therefore, both N-CoR and
SMRT can substitute for the endogenous corepressor(s) in mediating
COUP-TFI’s repressor function.
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DISCUSSION |
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TOPABSTRACTINTRODUCTIONRESULTSDISCUSSIONMATERIALS AND METHODSREFERENCES |
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35 (which has
lost its repression domain), can squelch the repression activity of
Gal4-COUP-TFI. Previously, we showed that a 15-amino-acid deletion from
the C terminus (Gal4-COUP-TF15) had little effect on Gal4-COUP-TF
activity, whereas a 25-amino-acid (Gal4-COUP-TF25) or a
35-amino-acid (Gal4-COUP-TF35) deletion largely impaired its active
repression function (27). Therefore, these data suggested that the
C-terminal border of the major active repression function of COUP-TF is
located within amino acids 408 and 398, and it is this region that may
interact with the corepressor(s). In addition, the repressor domain of
COUP-TFI may directly target the basal transcriptional machinery.
To examine whether a corepressor(s) can be shared between TRß and
COUP-TFI, squelching experiments were performed. As shown in Fig. 2, unliganded but not liganded TRß can squelch the basal repression of
Gal4-COUP-TFI. The evidence that the TR mutant, TR168–456
(V174A/D177A) (28), which does not interact with the putative
corepressors, cannot squelch the basal repression of Gal4-COUP-TFI
further supports the notion that common corepressors may be involved in
basal repression between TRß and COUP-TFI. Furthermore,
overexpression of COUP-TFI, but not COUP-TFI35, can squelch the
basal repression activity of Gal4-TRß, also suggesting that common
corepressors can function for both COUP-TFI and TRß. Theoretically,
the target of transcriptional interference may be either a basal
transcription factor(s) or a corepressor(s). Transfection of COUP-TFI
or TRß did not change the basal transcription of a PRE-tk-luciferase
reporter lacking a proper response element (data not shown), suggesting
that squelchers are unlikely to interfere directly with the function of
any basal transcriptional machinery. Therefore, the target(s) of
interference between COUP-TF and TRß is likely to be one or more
transcriptional corepressor protein(s).
Because COUP-TFI can form homodimers by itself or form heterodimers
with TRß (27), it is possible that the squelchers can form
non-DNA-binding heterodimers with the repressors used in Figs. 1, 2, and 3 (Gal4-COUP-TFI/COUP-TFI for Fig. 1, Gal4-COUP-TFI/TRß for Fig. 2, and Gal4-TRß/COUP-TFI for Fig. 3). If this is the case, inhibition
of repressor activity may be due to inhibition of DNA binding rather
than to squelching of a limiting corepressor(s). However, several lines
of evidence suggest that this is not the case. First, both COUP-TFI and
TRß have the ability to bind specifically to corepressors. Second, a
mutant form of TRß (TR168–456 (V174A/D177A)), which loses its
ability to interact with corepressor but retains its intact
dimerization domain, is not able to inhibit the repression activity of
Gal4-COUP-TFI. Third, COUP-TF mutant (COUP-TFI35), which loses its
ability in silencing, also loses its ability to squelch repressor
activity of TRß. Finally and most importantly, we have demonstrated
directly that both N-CoR and SMRT can mediate repressor activity of
COUP-TFI (Fig. 6) and reverse the self-squelching activity (Fig. 7).
Therefore, inhibition of repression activity by squelchers in Figs. 1, 2, and 3 indeed results from squelching of a limiting
corepressor(s).
Because squelching experiments showed that COUP-TFI may share a
corepressor(s) with TRß, we examined protein-protein interaction
between COUP-TFI and N-CoR or SMRT in a yeast two-hybrid assay and in
in vitro GST pull-down assays as shown in Figs. 4 and 5. The
amino acid 921-2453 fragment of N-CoR interacts with COUP-TFI. This
result is consistent with what has been observed in TR interaction
studies (10, 33). Interaction between COUP-TFI and the amino acid
190-2453 fragment of N-CoR was not detected in a yeast two-hybrid
assay, but was detected in an in vitro GST pull-down assay.
This discrepancy is likely due to the potent repressor domain of the
N-terminal portion of N-CoR, which suppresses the Gal4 activation
function, resulting in interference with ß-galactosidase expression.
Consistent with this interpretation, Seol et al. (33) also
recently demonstrated that the repressor domain of N-CoR strongly
interferes with the mammalian two-hybrid assay to study the
protein-protein interaction between N-CoR and TR or RAR. On the other
hand, the amino acid 29–564 and amino acid 565-1289, but not amino
acid 1192–1495, fragments of SMRT strongly interact with COUP-TF in
yeast and in vitro assays. Based on these data, we concluded
that there are at least two COUP-TFI-interacting domains within the
SMRT molecules. The lack of interaction between COUP-TFI and SMRT
(1192–1495) is surprising because this region interacts very strongly
with TRß. Thus, different repressors may interact differentially with
SMRT. Finally, the corepressor-interacting region in COUP-TFI is
localized in the extreme C terminus, which is quite different from the
region of TR and RAR where hinge and N-terminal portions of LBD are
involved in this interaction. Thus, repression function of COUP-TFs may
act in a different way from that of TR and RAR (Fig. 8).
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. Recently, an activator for COUP-TFII has been identified using a yeast two-hybrid screen, designated ORCA (orphan receptor coactivator) (35), and this factor is identical to a recently described ligand (p62) of tyrosine kinase- signaling molecule p56lck, suggesting that ORCA may link COUP-TFII and cell surface signal transduction pathways. This integrating role may be similar to what is observed with cAMP response element-binding protein CBP and the related protein p300. CBP plays a role in integrating cAMP second messenger and nuclear hormone receptor signal transduction pathways. Of interest, ORCA/p62 shares a small region of homology with CBP, suggesting a potential similarity in their mechanism of action. However, based on their data, ORCA/p62 does not bind directly to COUP-TFII-binding sites and COUP-TFII/ORCA complex is not detected in gel retardation assays. Therefore, it is possible that ORCA/p62 may function directly or indirectly by phosphorylating COUP-TFII or ORCA/p62 may overcome the function of a specific COUP-TFII-associated corepressor. Because ORCA/p62 can convert COUP-TFII into a transcriptional activator in a ligand-independent manner in mammalian cells, it is possible that COUP-TFI can also be activated by a coactivator(s) in a ligand-independent manner. Our preliminary data showed that overexpression of hSRC-1a (36), which is a general coactivator for members of steroid receptors, cannot relieve the repressor activity of Gal4-COUP-TFI in HeLa cells (data not shown).
In conclusion, we demonstrated that corepressors are involved in the mechanisms of COUP-TFI-mediated gene silencing, and that both N-CoR and SMRT can function as corepressors for COUP-TFI in mammalian cells. Therefore, orphan receptors such as COUP-TFI and RevErb A can function as a repressor in vivo by utilizing corepressors that are common for members of the TR and RAR subfamily.
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MATERIALS AND METHODS |
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TOPABSTRACTINTRODUCTIONRESULTSDISCUSSIONMATERIALS AND METHODSREFERENCES |
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Cloning of SMRT by Yeast Two-Hybrid System
Yeast strains used are as follows. y190:
MATa, leu2–3, 112,
ura3–52, trp1–901, his2-D200, ade2–101,
gal4gal180URA3 GAL-lacZ, LYS GAL-HIS3,
cyhr. y187: MAT
, gal4, gal80,
his3, trp1–901, ade2–101, ura3–52, leu2–3, -112, URA3 GAL-lacZ
met-. BJ2168: MATa, prc1–407, Prb1–1122,
pep4–3, leu2, trp1, ura 3–52. Yeast-selective media and plates
were prepared according to Guthrie and Fink (37). The yeast strain y190
containing pAS1cyh2-TR168–456 was transformed with a human brain cDNA
library in pGAD10 (Clontech, Palo Alto, CA) and plated on synthetic
complete medium lacking tryptophan, leucine, and histidine (containing
25 mM 3-aminotriazole) as described by Durfee et
al. (38). His+ colonies exhibiting ß-galactosidase
activity using the filter lift assay were further characterized.
ß-Galactosidase activity was determined using chlorophenol red
ß-D galactopyranoside as described (38). To recover the
library plasmids, total DNA from yeast was isolated and used to
transform Escherichia coli (HB101) which lacks
leu2 gene. Transformants were identified on minimal medium
lacking leucine and containing ampicillin. To ensure that the correct
cDNAs were identified, library plasmids isolated were retransformed
into y190 containing pAS1cyh2-TR168–456, and ß-galactosidase
activity was determined. The specificity of the interaction of cor 10.1
(SMRT 1192–1495), one of the 12 positive clones, with TR was
determined by mating y190 containing pGAD10-cor 10.1 with the strain
y187 containing either pAS1-SNF, pAS1-cdk2, pAS1-p53, or pAS1-lamin.
The ß-galactosidase activity of these diploids was examined using the
filter lift and chlorophenyl red ß-D galactopyranoside
methods. The cor 10.1 clone was identical to recently identified
corepressor SMRT. The yeast two-hybrid system was also used to
determine protein-protein interaction between COUP-TFI and SMRT or
N-CoR.
Protein-Protein Interaction by GST-Pulldown Assay
GST-COUP-TFI (pCBGST1-COUP-TFI) fusion protein was expressed and
extracted in yeast strain BJ2168 as described previously (39).
GST-pulldown assay was performed as described with modifications (4, 39): 30 µl glutathione-Sepharose beads stored in NENT buffer (500
mM NaCl, 1 mM EDTA, 20 mM Tris, pH
8.0, 0.5% NP-40, 1 mM dithiothreitol, 6 mM
MgCl2, and 8% glycerol) were incubated with yeast extracts
containing GST-fusion proteins in a 1:1 vol ratio together with NENT
buffer for 30–60 min at 4 C. Preparation of yeast extracts containing
GST-fusion protein was described previously (39). Subsequently, the
supernatant was removed and the beads were washed twice with 1 ml NENT
buffer and twice with 1 ml transcription washing buffer (60
mM NaCl, 1 mM EDTA, 20 mM Tris, pH
8.0, 0.05% NP-40, 1 mM dithiothreitol, 6 mM
MgCl2, and 8% glycerol). In vitro-translated and
-radiolabeled proteins were obtained using TNT Coupled Reticulocyte
Lysate Systems (Promega). Five to 10 µl crude lysate were incubated
with the beads in 200 µl transcription washing buffer for 2 h at
4 C. Finally, the beads were washed five times with 1 ml NENT buffer
and proteins were solubilized in SDS loading buffer and analyzed on
SDS-PAGE. The input lane contains 10% of the labeled protein used for
binding.
Plasmids
Mammalian Expression Vectors
The expression plasmids pABgal147, pABgal, pABgalTRß,
pABgalTRß, pABgal-TR168–456 (V174A/D177A), pRSV-COUP-TFI,
pRSV-COUP-TFI35, and pRSVgalCOUP-TFI were described previously (5, 20, 21, 27, 28, 40). pCMX-N-CoR (10) and pCMX-SMRT (12) were generous
gifts from Dr. A. J. Hörlein and Dr. J. D. Chen, respectively.
The 17 mer x 4-tk-LUC reporter gene contains four copies of a
17-mer upstream activating sequence located upstream of the thymidine
kinase promoter and luciferase gene. pCR3-SMRT565–1289 was constructed
by TA Cloning (Invitrogen) of PCR-amplified product with primers
5'-AGCTGACGTCGACGCCTCGTG-3' and 5'-CTGCACCGCCTGGCTTCTAT-3' in which
template cDNA was made by reverse transcription of human skeletal
muscle mRNA (Clontech) with primer 5'-GCTGGCATGTTCCTGCACCG-3'.
pCR3-SMRT565–1495 was constructed by inserting the EcoRI
(filled)-BglII fragment of pGAD10-SMRT1192–1495 into the
BglII-EcoRV site of pCR3-SMRT565–1289.
pCR3-SMRT29–564 was constructed by TA Cloning (Invitrogen) of
PCR-amplified product with primers 5'-AAGATTCCGAGCTCTGCTAC-3' and
5'-CACGAGGCGTCGACGTCAGC-3' in which template cDNA was made by reverse
transcription of human skeletal muscle mRNA (Clontech) with primer
5'-GTGCGGGGACTTGGCGATCT-3'. pCR3-SMRT29–1495 was constructed by
inserting the SalI fragment of pCR3-SMRT29–564 into the
SalI site of pCR3-SMRT565–1495. pABgalSMRT29–1495 was
constructed by inserting the SalI (partial)-XbaI
fragment into the PvuII site of pABgal. All PCR generates
clones were sequenced to ensure that no mutation occurred during PCR
reactions.
Yeast Vectors
The Gal4 DBD-TRß168–456 yeast expression plasmid
(pAS1cyh2-TR168–456) was constructed by inserting the
HindIII-SmaI blunt-ended fragment of
pABgalTR168–456 into the SmaI site of pAS1cyh2 (38).
The Gal4 DBD-COUP-TFI56–423 yeast expression plasmid
(pAS1cyh2-COUP-TFI) was constructed by inserting the
EcoRI-SmaI (filled) fragment of
pGEM7Zf(+)-COUP-TFI into the SmaI site of pAS1cyh2. Yeast
expression plasmid, pCBGST1-COUP-TFI56–423, was constructed by
inserting the EcoRI-SmaI (filled) fragment (amino
acids 56–423) of pGEM7Zf(+)-COUP-TFI into the SmaI site of
pCBGST1 (39). Yeast expression plasmid, pACTII-N-CoR190–2453, was
constructed by inserting the PvuI-SalI (filled)
fragment of pCMX-N-CoR into the NcoI-XhoI site
(filled) of pACTII (38). Yeast expression plasmid,
pACTII-N-CoR921–2453, was constructed by inserting the
HincII-SalI (filled) fragment of pCMX-N-CoR into
the SmaI site of pACTII. pACTII-SMRT29–564 was constructed
by inserting the SalI fragment (filled) of pCR3-SMRT29–564
into the NcoI (filled) site of pACTII. pACTII-SMRT565–1495
was constructed by inserting the SalI-XhoI
fragment of pCR3-SMRT565–1495 into the NcoI (filled) site
of pACTII. Yeast expression plasmid, pGAD10-SMRT1192–1495, was
recovered from a yeast two-hybrid screen using pAS1cyh2-TR168–456 as a
bait. Yeast expression plasmid, pACTII-TFIIB, was constructed by
inserting the NcoI (partial)-EcoRI fragment of
pGST-TFIIB (4) into the NcoI-EcoRI sites of
pACTII.
In Vitro Transcription and Translation Vectors
pT7-N-CoR190–2453 was constructed by inserting the
PvuI-SalI fragment of pCMX-N-CoR into the
NcoI site (filled) of pT7ßSal (41). PT7-N-CoR921–2453 was
constructed by inserting the HincII-SalI fragment
of pCMX-N-CoR into the AccI site (filled) of pT7ßSal.
pT7-SMRT29–564 was constructed by inserting the SalI
fragment (filled) of pCR3-SMRT29–564 into the
NcoI-EcoRI (filled) site of pT7ßSal.
pT7-SMRT565–1289 was constructed by inserting the
SalI-EcoRV fragment of pCR3-SMRT565–1289 into
the NcoI-EcoRI (filled) site of pT7ßSal.
PT7-SMRT1192–1495 was constructed by inserting the EcoRI
fragment (filled) of pGAD10-SMRT1192–1495 into the HincII
site of pT7ßSal. pT7-TFIIB was constructed by inserting the
NcoI (partial)-EcoRI fragment (filled) of
pGST-TFIIB (4) into the AccI site (filled) of pT7ßSal.
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ACKNOWLEDGMENTS |
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FOOTNOTES |
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This work was supported by NIH Grants (DK-45641 to M.J.T. and HD-08188 to B.W.O.).
Received for publication January 15, 1997. Accepted for publication February 14, 1997.
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REFERENCES |
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TOPABSTRACTINTRODUCTIONRESULTSDISCUSSIONMATERIALS AND METHODSREFERENCES |
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4 activation domain of the thyroid hormone receptor is
required for release of a putative corepressor(s) necessary for
transcriptional silencing. Mol Cell Biol 15:76–86[Abstract]
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 L.-j. Zhang, X. Liu, P. R. Gafken, C. Kioussi, and M. Leid A Chicken Ovalbumin Upstream Promoter Transcription Factor I (COUP-TFI) Complex Represses Expression of the Gene Encoding Tumor Necrosis Factor {alpha}-induced Protein 8 (TNFAIP8) J. Biol. Chem., March 6, 2009; 284(10): 6156 - 6168. [Abstract] [Full Text] [PDF]
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K. Yokota, H. Shibata, I. Kurihara, S. Kobayashi, N. Suda, A. Murai-Takeda, I. Saito, H. Kitagawa, S. Kato, T. Saruta, et al. Coactivation of the N-terminal Transactivation of Mineralocorticoid Receptor by Ubc9 J. Biol. Chem., January 19, 2007; 282(3): 1998 - 2010. [Abstract] [Full Text] [PDF]
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 G. Benoit, A. Cooney, V. Giguere, H. Ingraham, M. Lazar, G. Muscat, T. Perlmann, J.-P. Renaud, J. Schwabe, F. Sladek, et al. International Union of Pharmacology. LXVI. Orphan Nuclear Receptors Pharmacol. Rev., December 1, 2006; 58(4): 798 - 836. [Abstract] [Full Text] [PDF]
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 K. A. Riggs, N. S. Wickramasinghe, R. K. Cochrum, M. B. Watts, and C. M. Klinge Decreased Chicken Ovalbumin Upstream Promoter Transcription Factor II Expression in Tamoxifen-Resistant Breast Cancer Cells. Cancer Res., October 15, 2006; 66(20): 10188 - 10198. [Abstract] [Full Text] [PDF]
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 L. S. Tang, H. M. Alger, and F. A. Pereira COUP-TFI controls Notch regulation of hair cell and support cell differentiation Development, September 15, 2006; 133(18): 3683 - 3693. [Abstract] [Full Text] [PDF]
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 H.-G. Yoon and J. Wong The Corepressors Silencing Mediator of Retinoid and Thyroid Hormone Receptor and Nuclear Receptor Corepressor Are Involved in Agonist- and Antagonist-Regulated Transcription by Androgen Receptor Mol. Endocrinol., May 1, 2006; 20(5): 1048 - 1060. [Abstract] [Full Text] [PDF]
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X. Long and K. P. Nephew Fulvestrant (ICI 182,780)-dependent Interacting Proteins Mediate Immobilization and Degradation of Estrogen Receptor-{alpha} J. Biol. Chem., April 7, 2006; 281(14): 9607 - 9615. [Abstract] [Full Text] [PDF]
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 D. R. Johnson, C.-W. Li, L.-Y. Chen, J. C. Ghosh, and J. D. Chen Regulation and Binding of Pregnane X Receptor by Nuclear Receptor Corepressor Silencing Mediator of Retinoid and Thyroid Hormone Receptors (SMRT) Mol. Pharmacol., January 1, 2006; 69(1): 99 - 108. [Abstract] [Full Text] [PDF]
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 T. C. Voss, I. A. Demarco, C. F. Booker, and R. N. Day Functional interactions with Pit-1 reorganize co-repressor complexes in the living cell nucleus J. Cell Sci., August 1, 2005; 118(15): 3277 - 3288. [Abstract] [Full Text] [PDF]
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M. Beland and D. Lohnes Chicken Ovalbumin Upstream Promoter-Transcription Factor Members Repress Retinoic Acid-induced Cdx1 Expression J. Biol. Chem., April 8, 2005; 280(14): 13858 - 13862. [Abstract] [Full Text] [PDF]
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I. Kurihara, H. Shibata, S. Kobayashi, N. Suda, Y. Ikeda, K. Yokota, A. Murai, I. Saito, W. E. Rainey, and T. Saruta Ubc9 and Protein Inhibitor of Activated STAT 1 Activate Chicken Ovalbumin Upstream Promoter-Transcription Factor I-mediated Human CYP11B2 Gene Transcription J. Biol. Chem., February 25, 2005; 280(8): 6721 - 6730. [Abstract] [Full Text] [PDF]
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V. Kurtev, R. Margueron, K. Kroboth, E. Ogris, V. Cavailles, and C. Seiser Transcriptional Regulation by the Repressor of Estrogen Receptor Activity via Recruitment of Histone Deacetylases J. Biol. Chem., June 4, 2004; 279(23): 24834 - 24843. [Abstract] [Full Text] [PDF]
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M. J. Calonge, J. Seoane, and J. Massague Opposite Smad and Chicken Ovalbumin Upstream Promoter Transcription Factor Inputs in the Regulation of the Collagen VII Gene Promoter by Transforming Growth Factor-{beta} J. Biol. Chem., May 28, 2004; 279(22): 23759 - 23765. [Abstract] [Full Text] [PDF]
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M. U. De Martino, N. Bhattachryya, S. Alesci, T. Ichijo, G. P. Chrousos, and T. Kino The Glucocorticoid Receptor and the Orphan Nuclear Receptor Chicken Ovalbumin Upstream Promoter-Transcription Factor II Interact with and Mutually Affect Each Other's Transcriptional Activities: Implications for Intermediary Metabolism Mol. Endocrinol., April 1, 2004; 18(4): 820 - 833. [Abstract] [Full Text] [PDF]
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 Y. Zhang and M. L. Dufau Repression of the Luteinizing Hormone Receptor Gene Promoter by Cross Talk among EAR3/COUP-TFI, Sp1/Sp3, and TFIIB Mol. Cell. Biol., October 1, 2003; 23(19): 6958 - 6972. [Abstract] [Full Text] [PDF]
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S. Kang, N. J. Spann, T. Y. Hui, and R. A. Davis ARP-1/COUP-TF II Determines Hepatoma Phenotype by Acting as Both a Transcriptional Repressor of Microsomal Triglyceride Transfer Protein and an Inducer of CYP7A1 J. Biol. Chem., August 15, 2003; 278(33): 30478 - 30486. [Abstract] [Full Text] [PDF]
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M. D. Westfall, D. J. Mays, J. C. Sniezek, and J. A. Pietenpol The {Delta}Np63{alpha} Phosphoprotein Binds the p21 and 14-3-3{sigma} Promoters In Vivo and Has Transcriptional Repressor Activity That Is Reduced by Hay-Wells Syndrome-Derived Mutations Mol. Cell. Biol., April 1, 2003; 23(7): 2264 - 2276. [Abstract] [Full Text] [PDF]
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Y. Yang, X. Wang, T. Dong, E. Kim, W.-J. Lin, and C. Chang Identification of a Novel Testicular Orphan Receptor-4 (TR4)-associated Protein as Repressor for the Selective Suppression of TR4-mediated Transactivation J. Biol. Chem., February 21, 2003; 278(9): 7709 - 7717. [Abstract] [Full Text] [PDF]
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G. Liao, L.-Y. Chen, A. Zhang, A. Godavarthy, F. Xia, J. C. Ghosh, H. Li, and J. D. Chen Regulation of Androgen Receptor Activity by the Nuclear Receptor Corepressor SMRT J. Biol. Chem., February 7, 2003; 278(7): 5052 - 5061. [Abstract] [Full Text] [PDF]
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Y.-Y. Liu and G. A. Brent A Complex Deoxyribonucleic Acid Response Element in the Rat Ca2+/Calmodulin-Dependent Protein Kinase IV Gene 5'-Flanking Region Mediates Thyroid Hormone Induction and Chicken Ovalbumin Upstream Promoter Transcription Factor 1 Repression Mol. Endocrinol., November 1, 2002; 16(11): 2439 - 2451. [Abstract] [Full Text] [PDF]
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G. B. Potter, J. M. Zarach, J. M. Sisk, and C. C. Thompson The Thyroid Hormone-Regulated Corepressor Hairless Associates with Histone Deacetylases in Neonatal Rat Brain Mol. Endocrinol., November 1, 2002; 16(11): 2547 - 2560. [Abstract] [Full Text] [PDF]
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A. N. Moraitis, V. Giguere, and C. C. Thompson Novel Mechanism of Nuclear Receptor Corepressor Interaction Dictated by Activation Function 2 Helix Determinants Mol. Cell. Biol., October 1, 2002; 22(19): 6831 - 6841. [Abstract] [Full Text] [PDF]
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F. Lin, S. K. Kolluri, G.-q. Chen, and X.-k. Zhang Regulation of Retinoic Acid-induced Inhibition of AP-1 Activity by Orphan Receptor Chicken Ovalbumin Upstream Promoter-Transcription Factor J. Biol. Chem., June 7, 2002; 277(24): 21414 - 21422. [Abstract] [Full Text] [PDF]
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K. Jepsen and M. G. Rosenfeld Biological roles and mechanistic actions of co-repressor complexes J. Cell Sci., February 15, 2002; 115(4): 689 - 698. [Abstract] [Full Text] [PDF]
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A. Marimuthu, W. Feng, T. Tagami, H. Nguyen, J. L. Jameson, R. J. Fletterick, J. D. Baxter, and B. L. West TR Surfaces and Conformations Required to Bind Nuclear Receptor Corepressor Mol. Endocrinol., February 1, 2002; 16(2): 271 - 286. [Abstract] [Full Text] [PDF]
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Y. Zhang and M. L. Dufau EAR2 and EAR3/COUP-TFI Regulate Transcription of the Rat LH Receptor Mol. Endocrinol., November 1, 2001; 15(11): 1891 - 1905. [Abstract] [Full Text] [PDF]
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J. M. Amann, J. Nip, D. K. Strom, B. Lutterbach, H. Harada, N. Lenny, J. R. Downing, S. Meyers, and S. W. Hiebert ETO, a Target of t(8;21) in Acute Leukemia, Makes Distinct Contacts with Multiple Histone Deacetylases and Binds mSin3A through Its Oligomerization Domain Mol. Cell. Biol., October 1, 2001; 21(19): 6470 - 6483. [Abstract] [Full Text] [PDF]
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 A. Aranda and A. Pascual Nuclear Hormone Receptors and Gene Expression Physiol Rev, July 1, 2001; 81(3): 1269 - 1304. [Abstract] [Full Text] [PDF]
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X. Hu, Y. Li, and M. A. Lazar Determinants of CoRNR-Dependent Repression Complex Assembly on Nuclear Hormone Receptors Mol. Cell. Biol., March 1, 2001; 21(5): 1747 - 1758. [Abstract] [Full Text]
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E. C. Forsberg, K. M. Downs, H. M. Christensen, H. Im, P. A. Nuzzi, and E. H. Bresnick Developmentally dynamic histone acetylation pattern of a tissue-specific chromatin domain PNAS, December 19, 2000; 97(26): 14494 - 14499. [Abstract] [Full Text] [PDF]
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Y.-D. Wen, V. Perissi, L. M. Staszewski, W.-M. Yang, A. Krones, C. K. Glass, M. G. Rosenfeld, and E. Seto The histone deacetylase-3 complex contains nuclear receptor corepressors PNAS, June 20, 2000; 97(13): 7202 - 7207. [Abstract] [Full Text] [PDF]
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D. Avram, A. Fields, K. P. O. Top, D. J. Nevrivy, J. E. Ishmael, and M. Leid Isolation of a Novel Family of C2H2 Zinc Finger Proteins Implicated in Transcriptional Repression Mediated by Chicken Ovalbumin Upstream Promoter Transcription Factor (COUP-TF) Orphan Nuclear Receptors J. Biol. Chem., March 31, 2000; 275(14): 10315 - 10322. [Abstract] [Full Text] [PDF]
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T. Sugiyama, J.-C. Wang, D. K. Scott, and D. K. Granner Transcription Activation by the Orphan Nuclear Receptor, Chicken Ovalbumin Upstream Promoter-Transcription Factor I (COUP-TFI). DEFINITION OF THE DOMAIN INVOLVED IN THE GLUCOCORTICOID RESPONSE OF THE PHOSPHOENOLPYRUVATE CARBOXYKINASE GENE J. Biol. Chem., February 4, 2000; 275(5): 3446 - 3454. [Abstract] [Full Text] [PDF]
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Y. Zhang and M. L. Dufau Nuclear Orphan Receptors Regulate Transcription of the Gene for the Human Luteinizing Hormone Receptor J. Biol. Chem., January 28, 2000; 275(4): 2763 - 2770. [Abstract] [Full Text] [PDF]
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 C. K. Glass and M. G. Rosenfeld The coregulator exchange in transcriptional functions of nuclear receptors Genes & Dev., January 15, 2000; 14(2): 121 - 141. [Full Text]
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H.-b. Lin, M. Jurk, T. Gulick, and G. M. Cooper Identification of COUP-TF as a Transcriptional Repressor of the c-mos Proto-oncogene J. Biol. Chem., December 17, 1999; 274(51): 36796 - 36800. [Abstract] [Full Text] [PDF]
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V. Perissi, L. M. Staszewski, E. M. McInerney, R. Kurokawa, A. Krones, D. W. Rose, M. H. Lambert, M. V. Milburn, C. K. Glass, and M. G. Rosenfeld Molecular determinants of nuclear receptor-corepressor interaction Genes & Dev., December 15, 1999; 13(24): 3198 - 3208. [Abstract] [Full Text]
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K. Yanai, K. Hirota, K. Taniguchi-Yanai, Y. Shigematsu, Y. Shimamoto, T. Saito, S. Chowdhury, M. Takiguchi, M. Arakawa, Y. Nibu, et al. Regulated Expression of Human Angiotensinogen Gene by Hepatocyte Nuclear Factor 4 and Chicken Ovalbumin Upstream Promoter-Transcription Factor J. Biol. Chem., December 3, 1999; 274(49): 34605 - 34612. [Abstract] [Full Text] [PDF]
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L.-J. Chew, F. Huang, J.-M. Boutin, and V. Gallo Identification of Nuclear Orphan Receptors as Regulators of Expression of a Neurotransmitter Receptor Gene J. Biol. Chem., October 8, 1999; 274(41): 29366 - 29375. [Abstract] [Full Text] [PDF]
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 B. Desvergne and W. Wahli Peroxisome Proliferator-Activated Receptors: Nuclear Control of Metabolism Endocr. Rev., October 1, 1999; 20(5): 649 - 688. [Abstract] [Full Text]
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V. Giguère Orphan Nuclear Receptors: From Gene to Function Endocr. Rev., October 1, 1999; 20(5): 689 - 725. [Abstract] [Full Text]
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R. Fenrick, J. M. Amann, B. Lutterbach, L. Wang, J. J. Westendorf, J. R. Downing, and S. W. Hiebert Both TEL and AML-1 Contribute Repression Domains to the t(12;21) Fusion Protein Mol. Cell. Biol., October 1, 1999; 19(10): 6566 - 6574. [Abstract] [Full Text] [PDF]
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D.-Q. Lou, M. Tannour, L. Selig, D. Thomas, A. Kahn, and M. Vasseur-Cognet Chicken Ovalbumin Upstream Promoter-Transcription Factor II, a New Partner of the Glucose Response Element of the L-type Pyruvate Kinase Gene, Acts as an Inhibitor of the Glucose Response J. Biol. Chem., October 1, 1999; 274(40): 28385 - 28394. [Abstract] [Full Text] [PDF]
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N. J. McKenna, R. B. Lanz, and B. W. O’Malley Nuclear Receptor Coregulators: Cellular and Molecular Biology Endocr. Rev., June 1, 1999; 20(3): 321 - 344. [Abstract] [Full Text]
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D. Avram, J. E. Ishmael, D. J. Nevrivy, V. J. Peterson, S.-H. Lee, P. Dowell, and M. Leid Heterodimeric Interactions between Chicken Ovalbumin Upstream Promoter-Transcription Factor Family Members ARP1 and Ear2 J. Biol. Chem., May 14, 1999; 274(20): 14331 - 14336. [Abstract] [Full Text] [PDF]
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U. Dressel, D. Thormeyer, B. Altincicek, A. Paululat, M. Eggert, S. Schneider, S. P. Tenbaum, R. Renkawitz, and A. Baniahmad Alien, a Highly Conserved Protein with Characteristics of a Corepressor for Members of the Nuclear Hormone Receptor Superfamily Mol. Cell. Biol., May 1, 1999; 19(5): 3383 - 3394. [Abstract] [Full Text] [PDF]
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C. Pipaon, S. Y. Tsai, and M.-J. Tsai COUP-TF Upregulates NGFI-A Gene Expression through an Sp1 Binding Site Mol. Cell. Biol., April 1, 1999; 19(4): 2734 - 2745. [Abstract] [Full Text] [PDF]
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 R. Nicol, G. Zheng, P. Sutrave, D. N. Foster, and E. Stavnezer Association of Specific DNA Binding and Transcriptional Repression with the Transforming and Myogenic Activities of c-Ski Cell Growth Differ., April 1, 1999; 10(4): 243 - 254. [Abstract] [Full Text]
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 C. E. Robinson, X. Wu, Z. Nawaz, S. A. Onãte, and J. M. Gimble A Corepressor and Chicken Ovalbumin Upstream Promoter Transcriptional Factor Proteins Modulate Peroxisome Proliferator-Activated Receptor-{gamma}2/Retinoid X Receptor {alpha}-Activated Transcription from the Murine Lipoprotein Lipase Promoter Endocrinology, April 1, 1999; 140(4): 1586 - 1593. [Abstract] [Full Text]
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E.-J. Park, D. J. Schroen, M. Yang, H. Li, L. Li, and J. D. Chen SMRTe, a silencing mediator for retinoid and thyroid hormone receptors-extended isoform that is more related to the nuclear receptor corepressor PNAS, March 30, 1999; 96(7): 3519 - 3524. [Abstract] [Full Text] [PDF]
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K. Zeitoun, K. Takayama, M. D. Michael, and S. E. Bulun Stimulation of Aromatase P450 Promoter (II) Activity in Endometriosis and Its Inhibition in Endometrium Are Regulated by Competitive Binding of Steroidogenic Factor-1 and Chicken Ovalbumin Upstream Promoter Transcription Factor to the Same cis-Acting Element Mol. Endocrinol., February 1, 1999; 13(2): 239 - 253. [Abstract] [Full Text]
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S.-H. Hong and M. L. Privalsky Retinoid Isomers Differ in the Ability to Induce Release of SMRT Corepressor from Retinoic Acid Receptor-alpha J. Biol. Chem., January 29, 1999; 274(5): 2885 - 2892. [Abstract] [Full Text] [PDF]
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C.-H. Lee, C. Chinpaisal, and L.-N. Wei Cloning and Characterization of Mouse RIP140, a Corepressor for Nuclear Orphan Receptor TR2 Mol. Cell. Biol., November 1, 1998; 18(11): 6745 - 6755. [Abstract] [Full Text]
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C.-W. Wong and M. L. Privalsky Components of the SMRT Corepressor Complex Exhibit Distinctive Interactions with the POZ Domain Oncoproteins PLZF, PLZF-RARalpha , and BCL-6 J. Biol. Chem., October 16, 1998; 273(42): 27695 - 27702. [Abstract] [Full Text] [PDF]
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C.-W. Wong and M. L. Privalsky Transcriptional Silencing Is Defined by Isoform- and Heterodimer-Specific Interactions between Nuclear Hormone Receptors and Corepressors Mol. Cell. Biol., October 1, 1998; 18(10): 5724 - 5733. [Abstract] [Full Text]
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J. Leers, E. Treuter, and J.-A. Gustafsson Mechanistic Principles in NR Box-Dependent Interaction between Nuclear Hormone Receptors and the Coactivator TIF2 Mol. Cell. Biol., October 1, 1998; 18(10): 6001 - 6013. [Abstract] [Full Text]
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C.-W. Wong and M. L. Privalsky Transcriptional Repression by the SMRT-mSin3 Corepressor: Multiple Interactions, Multiple Mechanisms, and a Potential Role for TFIIB Mol. Cell. Biol., September 1, 1998; 18(9): 5500 - 5510. [Abstract] [Full Text]
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S.-H. Hong, C.-W. Wong, and M. L. Privalsky Signaling by Tyrosine Kinases Negatively Regulates the Interaction between Transcription Factors and SMRT (Silencing Mediator of Retinoic Acid and Thyroid Hormone Receptor) Corepressor Mol. Endocrinol., August 1, 1998; 12(8): 1161 - 1171. [Abstract] [Full Text]
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R. N. Yu, M. Ito, and J. L. Jameson The Murine Dax-1 Promoter Is Stimulated by SF-1 (Steroidogenic Factor-1) and Inhibited by COUP-TF (Chicken Ovalbumin Upstream Promoter-Transcription Factor) via a Composite Nuclear Receptor-Regulatory Element Mol. Endocrinol., July 1, 1998; 12(7): 1010 - 1022. [Abstract] [Full Text]
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J. Zhang, M. G. Guenther, R. W. Carthew, and M. A. Lazar Proteasomal regulation of nuclear receptor corepressor-mediated repression Genes & Dev., June 15, 1998; 12(12): 1775 - 1780. [Abstract] [Full Text]
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E. Treuter, T. Albrektsen, L. Johansson, J. Leers, and J.-A. Gustafsson A Regulatory Role for RIP140 in Nuclear Receptor Activation Mol. Endocrinol., June 1, 1998; 12(6): 864 - 881. [Abstract] [Full Text]
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P. A. Crawford, C. Dorn, Y. Sadovsky, and J. Milbrandt Nuclear Receptor DAX-1 Recruits Nuclear Receptor Corepressor N-CoR to Steroidogenic Factor 1 Mol. Cell. Biol., May 1, 1998; 18(5): 2949 - 2956. [Abstract] [Full Text]
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C. M. Klinge, B. F. Silver, M. D. Driscoll, G. Sathya, R. A. Bambara, and R. Hilf Chicken Ovalbumin Upstream Promoter-Transcription Factor Interacts with Estrogen Receptor, Binds to Estrogen Response Elements and Half-Sites, and Inhibits Estrogen-induced Gene Expression J. Biol. Chem., December 12, 1997; 272(50): 31465 - 31474. [Abstract] [Full Text] [PDF]
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Z. Yan and A. M. Jetten Characterization of the Repressor Function of the Nuclear Orphan Receptor Retinoid Receptor-related Testis-associated Receptor/Germ Cell Nuclear Factor J. Biol. Chem., November 3, 2000; 275(45): 35077 - 35085. [Abstract] [Full Text] [PDF]
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X. Feng, Y. Jiang, P. Meltzer, and P. M. Yen Transgenic Targeting of a Dominant Negative Corepressor to Liver Blocks Basal Repression by Thyroid Hormone Receptor and Increases Cell Proliferation J. Biol. Chem., April 27, 2001; 276(18): 15066 - 15072. [Abstract] [Full Text] [PDF]
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G. S. Huggins, C. J. Bacani, J. Boltax, R. Aikawa, and J. M. Leiden Friend of GATA 2 Physically Interacts with Chicken Ovalbumin Upstream Promoter-TF2 (COUP-TF2) and COUP-TF3 and Represses COUP-TF2-dependent Activation of the Atrial Natriuretic Factor Promoter J. Biol. Chem., July 20, 2001; 276(30): 28029 - 28036. [Abstract] [Full Text] [PDF]
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