| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
J Biol Chem, Vol. 273, Issue 44, 28564-28567, October 30, 1998
,¶
From the College of Pharmacy and ¶ Hormone
Research Center, Chonnam National University, Kwangju 500-757, Korea
and the § Institute of Environmental and Life Sciences,
Hallym University, Chuncheon 200-702, Korea
 |
ABSTRACT |
|---|
Top
Abstract
Introduction
Procedures
Results & Discussion
References
|
|---|
Steroid receptor coactivator-1 (SRC-1)
specifically bound to serum response factor (SRF), as demonstrated by
glutathione S-transferase pull down assays, and the yeast
and mammalian two-hybrid tests. In mammalian cells, SRC-1 potentiated
serum response element (SRE)-mediated transactivations in a
dose-dependent manner. Coexpression of p300 synergistically
enhanced this SRC-1-potentiated level of transactivations, consistent
with the recent finding (Ramirez, S., Ali, S. A. S., Robin,
P., Trouche, D., and Harel-Bellan, A. (1997) J. Biol.
Chem. 272, 31016-31021) in which the p300 homologue CREB-binding
protein was shown to be a transcription coactivator of SRF. Thus, we
concluded that at least two distinct classes of coactivator molecules
may cooperate to regulate SRF-dependent transactivations
in vivo.
The serum response element
(SRE)1 (1) is present in the
upstream regulatory sequences of a number of immediate early genes such
as c-fos (2, 3). The SRE is constitutively occupied by a
complex of two proteins, serum response factor (SRF) (4) and ternary
complex factor (TCF) (5). SRF belongs to the MADS box family of
proteins (6) and recognizes a CArG box in the SRE (7). TCF does not
bind autonomously to the element, but requires the assistance of SRF to
efficiently contact the DNA (8, 9). The sequence recognized by TCF,
located upstream of the CArG box, is in the form of CAGGA, a sequence
that binds proteins from the Ets family. Several Ets proteins display a
TCF activity on the c-fos SRE: ELK-1 (10), SAP-1 (11), and
SAP-2/NET/ERP (12, 13). In addition, the SRE is recognized by oncogenic fusion proteins such as EWS-FL1 (14). Both SRF and TCF contain a
transactivation domain (15, 16). SRF is a direct target for a poorly
defined signal transduction pathway (17), whereas transactivation by
TCF is induced by mitogens (18, 19). Transactivation domains of TCFs
are direct targets for the Ras/MAP kinase transduction pathway and are
substrates for ERK-1 and ERK-2 (20-22), suggesting that
phosphorylation by MAP kinases activates these domains.
Transcription coactivators bridge transcription factors and the
components of the basal transcriptional apparatus (23). Functionally
conserved proteins CREB binding protein (CBP) and p300 have been shown
to be essential for the activation of transcription by a large number
of regulated transcription factors, including nuclear receptors
(24-27), CREB (28-30), NF In light of the fact that SRC-1 is capable of forming a complex with
CBP and p300 that in turn coactivates the c-fos SRE through TCF (38) and SRF (39), we tested whether SRC-1 itself participates in
the SRE-mediated transactivations as well. Herein, we show that 1)
SRC-1 specifically binds to SRF, 2) SRC-1 coactivates the SRE-mediated
transactivations, and 3) p300 synergizes with SRC-1 in this
coactivation. These results suggest that at least two distinct classes
of coactivator molecules (i.e. SRC-1 and CBP/p300) may
cooperate to regulate SRF-dependent transactivations in vivo.
Plasmids--
T7 and B42 vectors to express SRC-1 and fragments
of SRC-1 (SRC-A to SRC-E as depicted in Fig. 3) were as described
previously (57, 58). An XbaI-BamHI fragment
encoding a full-length SRF was filled in by Klenow fragment and dNTPs
and subcloned into a SmaI restriction site of pGEX4T
(Amersham Pharmacia Biotech) to express GST/SRF. A polymerase chain
reaction-amplified fragment encoding a full-length SRF was cloned into
EcoRI and XhoI restriction sites of pJG4-5 to
express B42/SRF. The VP16/SRC-1 expression vector was a gift of Dr.
Ming Tsai (Baylor College of Medicine, Houston, TX). The mammalian
expression vectors for p300, SRC-1, SRF, and Gal4-SRF along with the
transfection indicator construct pRSV- GST-Pull Down Assays--
The GST-fusions or GST alone was
expressed in Escherichia coli, bound to
glutathione-Sepharose 4B beads (Amersham Pharmacia Biotech), and
incubated with labeled proteins expressed by in vitro
translation by using the TNT-coupled
transcription-translation system, with conditions as described by the
manufacturer (Promega, Madison, WI). Specifically bound proteins were
eluted from beads with 40 mM reduced glutathione in 50 mM Tris (pH 8.0) and analyzed by SDS-polyacrylamide gel
electrophoresis and autoradiography as described (61).
Cell Culture and Transfections--
HeLa cells were grown in
24-well plates with medium supplemented with 10% fetal calf serum for
24 h and transfected with 100 ng of LacZ expression
vector pRSV- Interactions of SRC-1 and SRF--
We and others have recently
found that SRC-1 (26, 41) or its homologue p/CIP (48), originally
identified as a coactivator of nuclear receptors, also functions as a
coactivator of NF
To independently prove these interactions in vivo, we
exploited the mammalian two-hybrid tests (62). Consistent with the existence of a strong transcriptional repressive domain at the N-terminal sequences (16), Gal4 fusion protein to a full-length SRF
(Gal4-SRF) significantly repressed the basal level of transcription directed by Gal4 alone (data not shown). The Gal4-SRF-mediated transactivation, however, was stimulated by coexpression of VP16-SRC-1, but not VP16 alone, in a dose-dependent manner with
cotransfection of 100 ng of VP16/SRC-1 increasing the fold activation
approximately 3-fold, indicating that SRC-1 specifically interacts with
SRF in vivo (Fig. 1C). In addition, these
interactions were also confirmed in the yeast two-hybrid tests (57, 58)
(Table I). Coexpression of a B42 fusion
to the full-length SRF further stimulated the LexA/SRC-D- and
LexA/SRC-E-mediated LacZ expressions, whereas coexpression
of a B42 alone was without any effects (Table I). Consistent with the
in vitro results, the LacZ expressions mediated by LexA fusions to SRC-A or -C were not stimulated by coexpression of
B42-SRF. However, the interaction of SRF with SRC-B, which was readily
detected in the GST-pull downs (Fig. 1B), was not observed
in yeast. This discrepancy is not currently understood but may reflect
the fundamental differences between two different assay systems. These
results, along with the mammalian two-hybrid and GST pull-down results,
suggest that SRC-1 directly associates with SRF through multiple
subregions of SRC-1.
Cotransfection of SRC-1 Stimulates SRE-mediated
Transactivations--
To assess the functional consequences of these
interactions, SRC-1 was cotransfected into HeLa cells along with a
reporter construct SRE-c-fos-TK-LUC. This reporter
construct, previously characterized to efficiently mediate the
SRE-mediated transactivations in various cell types, consists of a
minimal promoter from the c-fos gene and a single upstream
consensus SRE (60). Serum shock with 20% fetal calf serum resulted in
an approximately 10-fold increase in transactivation of this reporter
construct, relative to the level with non-shocked cells (data not
shown). Increasing amounts of cotransfected SRC-1 enhanced the reporter
gene expressions in an SRC-1 dose-dependent manner, with
cotransfection of 200 ng of SRC-1 increasing the fold activation
approximately 8-fold (Fig. 2). Consistent
with the reports that CBP and p300 are transcription coactivators of
SRF and TCF (38, 39), increasing amounts of cotransfected p300 also had
stimulatory effects on the reporter gene expressions, with
cotransfection of 50 ng of p300 increasing the fold activation
approximately 2-fold. Consistent with an idea that SRC-1 and p300
synergize to coactivate the SRE-mediated transactivations, coexpression
of p300 and SRC-1 dramatically increased the reporter gene expressions
above the levels observed with SRC-1 or p300 alone, with cotransfection
of 50 ng of p300 and 200 ng of SRC-1 increasing the fold activation
approximately 80-fold (Fig. 2B). In contrast, cotransfection
of SRC-1 did not affect the LacZ reporter expression of the
transfection indicator construct pRSV-
In summary, we have shown that SRC-1 interacts with SRF and coactivates
SRE-mediated transactivations in synergy with p300, which was also
shown to be a coactivator of SRF and TCF (38, 39). This synergy is
believed to reflect a cooperative recruitment of two different
coactivator molecules (i.e. SRC-1 and CBP-p300) by SRF and
TCF. It's possible that these two distinct histone acetyltransferases
(46, 49-51) either modify selective sites on the histone tails or act
in a concerted fashion to control different aspects of transcriptional
activation. These results, along with the recent reports in which SRC-1
and its homologue p/CIP were shown to be coactivators for NF
INTRODUCTION
Top
Abstract
Introduction
Procedures
Results & Discussion
References
B (31, 32), bHLH factors (33), STATs (34,
35), AP-1 (36, 37) and SRF/TCF (38, 39). In particular, the nuclear
receptor superfamily is a group of ligand-dependent
transcriptional regulatory proteins that function by binding to
specific DNA sequences named hormone response elements in promoters of
target genes (reviewed in Ref. 40). Transcriptional regulation by
nuclear receptors depends primarily upon a ligand-dependent
activation function, AF2, located in the C terminus and predicted to
undergo an allosteric change upon ligand binding (40). Consistent with
this, CBP and p300 have been found to interact directly with nuclear
receptors in a ligand- and AF2-dependent manner (24-27).
In addition, a series of factors that exhibit ligand- and
AF2-dependent binding to nuclear receptors have been
identified both biochemically and by expression cloning. Among these, a
group of highly related proteins have been shown to form a complex with
CBP and p300 and enhance transcriptional activation by several nuclear
receptors, i.e. steroid receptor coactivator-1 (SRC-1) (26,
41), xSRC-3 (42), AIB1 (43), TIF2 (44), RAC3 (45), ACTR (46), TRAM-1
(47), and p/CIP (48). Interestingly, SRC-1 (49) and its homologue ACTR
(46), along with CBP and p300 (50, 51), were recently shown to contain potent histone acetyltransferase activities themselves and associate with yet another histone acetyltransferase protein p/CAF (52). In
contrast, it was shown that SMRT (53) and N-CoR (54), nuclear receptor
corepressors, form complexes with Sin3 and histone deacetylase proteins
(55, 56). From these results it was suggested that chromatin remodeling
by cofactors may contribute, through histone acetylation-deacetylation,
to transcription factor-mediated transcriptional regulation.
EXPERIMENTAL PROCEDURES
Top
Abstract
Introduction
Procedures
Results & Discussion
References
-gal, a reporter construct
Gal4-TK-LUC, and the serum-responsive reporter construct
SRE-c-fos-LUC, were as described previously (57-62).
-gal and 100 ng of a reporter gene
SRE-c-fos-LUC or Gal4-TK-LUC, along with an increasing
amount of expression vectors for SRC-1, p300, or VP16/SRC-1. Total
amounts of expression vectors were kept constant by adding decreasing amounts of pcDNA3 to transfections containing increasing amounts of
the SRC-1, p300, or VP16/SRC-1 vector. These cells were incubated with
medium containing 0.5% fetal calf serum for 20 h. Cells were washed and refed with Dulbecco's modified Eagle's medium containing 20% fetal calf serum. Cells were harvested 4 h later, luciferase activity was assayed as described (61), and the results were normalized
to the LacZ expression. Similar results were obtained in
more than two similar experiments.
RESULTS AND DISCUSSION
Top
Abstract
Introduction
Procedures
Results & Discussion
References
B (57), AP-1 (58), CREB, and STAT1 (63). These
transcription factors were previously shown to require CBP and p300
(28-32, 34-37) that are capable of forming a complex with SRC-1.
Because CBP and p300 were also found to coactivate the c-fos
SRE through interactions with TCF (38) and SRF (39), we tested whether
SRC-1 itself functionally interacts with SRF by using the in
vitro glutathione S-transferase (GST) pull down assays.
GST alone and GST-fusion to SRF were expressed, purified, and tested
for interaction with in vitro translated luciferase and
SRC-1. As shown in Fig. 1A, the radiolabeled SRC-1 readily interacted with GST/SRF, but not with
GST alone, whereas the radiolabeled luciferase didn't bind any of the
GST proteins, as expected. In addition, SRC-B, SRC-D, and SRC-E, among
various SRC-1 fragments, specifically interacted with GST/SRF, but not
with GST alone (Fig. 1B).
View larger version (25K):
[in a new window]
Fig. 1.
Interactions of SRF with SRC-1.
Luciferase, SRC-1 (A), and a series of five SRC-1 fragments
(B) were labeled with [35S]methionine by
in vitro translation and incubated with glutathione beads
containing GST alone or GST/SRF as indicated. Beads were washed, and
specifically bound material was eluted with reduced glutathione and
resolved by SDS-polyacrylamide gel electrophoresis. Approximately
10-20% of total input was typically retained. C, HeLa
cells were transfected with LacZ expression vector and
VP16/ 
or an increasing amount of VP16/SRC-1-expression vector along
with a reporter gene Gal4-TK-LUC reporter and Gal4-SRF expression
vector (62), as indicated. Normalized luciferase expressions from
triplicate samples are presented relative to the LacZ
expressions, and the standard deviations are less than 5%.
Interactions of SRC-1 with SRF in yeast
-D-galactopyranoside, and reproducible results were
obtained using colonies from a separate transformation. +++, strongly
blue colonies after 2 days of incubation; ++, light blue colonies after
2 days of incubation; +, light blue colonies after more than 2 days of
incubation; , white
colonies.
-gal either in the presence or
absence of serum shock (data not shown).
View larger version (13K):
[in a new window]
Fig. 2.
Effects of SRC-1 and p300 cotransfection on
the SRE-mediated transactivations. HeLa cells were transfected
with LacZ expression vector, p300 expression vector, and
increasing amounts of SRC-1 expression vector along with a reporter
gene SRE-c-fos-LUC (60), as indicated. Cells were shocked
with 20% fetal calf serum before harvest, as described (59, 60).
Normalized luciferase expressions from triplicate samples are presented
relative to the LacZ expressions, and the standard
deviations are less than 5%.
B (57),
AP-1 (58), CREB, and STAT-1 (63), clearly demonstrate that SRC-1 is an integrator molecule like CBP and p300 (24-27) (Fig.
3). Thus, SRC-1 may regulate yet other
transcription factors, particularly ones already found to be regulated
by CBP and p300. Further characterization of these integrator molecules
should provide important insights into the multifactorial control of
biological processes under regulation of multiple signal transduction
pathways in vivo.
View larger version (11K):
[in a new window]
Fig. 3.
SRC-1 as an integrator. The full-length
human SRC-1 and a series of five SRC-1 fragments (57, 58) are as
depicted. The nuclear receptor-interacting (receptor),
CBP-p300-interacting (p300), basic helix-loop-helix/PAS
(bHLH/PAS), serine-threonine-rich (S/T-rich), and
glutamine-rich (Q) domains, along with the recently
identified histone acetyltransferase domain (HAT) (49), the
AP-1 components c-Jun and c-Fos binding domain (c-Jun/c-Fos)
(58), and the NF B component p50-binding domain (p50)
(57), are as indicated. The amino acid numbers for each construct are
shown. The SRF-binding domains among various SRC-1 fragments are
shaded, as + indicates interactions with SRF and means no interaction.
| |
ACKNOWLEDGEMENTS |
|---|
We thank Dr. Ming Tsai for the SRC-1 clones and Dr. David Livingston for the p300 mammalian expression vector.
| |
FOOTNOTES |
|---|
* This work was supported by Grants 96-0401-08-01-3 and HRC (to J. W. L.) from the Korea Science and Engineering Foundation and Grant GE 96-81/97-143 (to J. W. L.) from the academic research fund of the Ministry of Education, Republic of Korea.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
To whom correspondence should be addressed. Tel.:
82-62-530-2934; Fax: 82-62-530-0772; E-mail:
jlee{at}chonnam.chonnam.ac.kr.
The abbreviations used are: SRE, serum response element; SRF, serum response factor; TCF, ternary complex factor; CBP, CREB-binding protein; CREB, cAMP response element-binding protein; SRC-1, steroid receptor coactivator-1; GST, glutathione S-transferase; MAP, mitogen-activated protein.
| |
REFERENCES |
|---|
|
Top
Abstract
Introduction
Procedures
Results & Discussion
References
|
|---|
This article has been cited by other articles:
|
|
 |
|
  T. K S Ku and D. L Crowe Coactivator-mediated estrogen response in human squamous cell carcinoma lines J. Endocrinol., April 1, 2007; 193(1): 147 - 155. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 J. Yu and R. J. Koenig Induction of Type 1 Iodothyronine Deiodinase to Prevent the Nonthyroidal Illness Syndrome in Mice Endocrinology, July 1, 2006; 147(7): 3580 - 3585. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 P. Yi, R.-C. Wu, J. Sandquist, J. Wong, S. Y. Tsai, M.-J. Tsai, A. R. Means, and B. W. O'Malley Peptidyl-Prolyl Isomerase 1 (Pin1) Serves as a Coactivator of Steroid Receptor by Regulating the Activity of Phosphorylated Steroid Receptor Coactivator 3 (SRC-3/AIB1) Mol. Cell. Biol., November 1, 2005; 25(21): 9687 - 9699. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 S.-Q. Kuang, L. Liao, S. Wang, D. Medina, B. W. O'Malley, and J. Xu Mice Lacking the Amplified in Breast Cancer 1/Steroid Receptor Coactivator-3 Are Resistant to Chemical Carcinogen-Induced Mammary Tumorigenesis Cancer Res., September 1, 2005; 65(17): 7993 - 8002. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 H.-Y. Wu, Y. Hamamori, J. Xu, S. C. Chang, T. Saluna, M.-F. Chang, B. W. O'Malley, and L. Kedes Nuclear Hormone Receptor Coregulator GRIP1 Suppresses, whereas SRC1A and p/CIP Coactivate, by Domain-specific Binding of MyoD J. Biol. Chem., February 4, 2005; 280(5): 3129 - 3137. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
Y. B. Choi, J. K. Ko, and J. Shin The Transcriptional Corepressor, PELP1, Recruits HDAC2 and Masks Histones Using Two Separate Domains J. Biol. Chem., December 3, 2004; 279(49): 50930 - 50941. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
A. Goel and R. Janknecht Concerted Activation of ETS Protein ER81 by p160 Coactivators, the Acetyltransferase p300 and the Receptor Tyrosine Kinase HER2/Neu J. Biol. Chem., April 9, 2004; 279(15): 14909 - 14916. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 E. Tzortzakaki, C. Spilianakis, E. Zika, A. Kretsovali, and J. Papamatheakis Steroid Receptor Coactivator 1 Links the Steroid and Interferon {gamma} Response Pathways Mol. Endocrinol., December 1, 2003; 17(12): 2509 - 2518. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
J. Xu and Q. Li Review of the in Vivo Functions of the p160 Steroid Receptor Coactivator Family Mol. Endocrinol., September 1, 2003; 17(9): 1681 - 1692. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 H. W. Liu, A. J. Halayko, D. J. Fernandes, G. S. Harmon, J. A. McCauley, P. Kocieniewski, J. McConville, Y. Fu, S. M. Forsythe, P. Kogut, et al. The RhoA/Rho Kinase Pathway Regulates Nuclear Localization of Serum Response Factor Am. J. Respir. Cell Mol. Biol., July 1, 2003; 29(1): 39 - 47. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 J. A. Carson, W. J. Lee, J. McClung, and G. A. Hand Steroid receptor concentration in aged rat hindlimb muscle: effect of anabolic steroid administration J Appl Physiol, July 1, 2002; 93(1): 242 - 250. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
S. Giraud, F. Bienvenu, S. Avril, H. Gascan, D. M. Heery, and O. Coqueret Functional Interaction of STAT3 Transcription Factor with the Coactivator NcoA/SRC1a J. Biol. Chem., March 1, 2002; 277(10): 8004 - 8011. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
D. A. Tice, I. Soloviev, and P. Polakis Activation of the Wnt Pathway Interferes with Serum Response Element-driven Transcription of Immediate Early Genes J. Biol. Chem., February 15, 2002; 277(8): 6118 - 6123. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
C. M. Litterst and E. Pfitzner Transcriptional Activation by STAT6 Requires the Direct Interaction with NCoA-1 J. Biol. Chem., November 30, 2001; 276(49): 45713 - 45721. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 A. Aranda and A. Pascual Nuclear Hormone Receptors and Gene Expression Physiol Rev, July 1, 2001; 81(3): 1269 - 1304. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
S.-K. Lee, S.-Y. Jung, Y.-S. Kim, S.-Y. Na, Y. C. Lee, and J. W. Lee Two Distinct Nuclear Receptor-Interaction Domains and CREB-Binding Protein-Dependent Transactivation Function of Activating Signal Cointegrator-2 Mol. Endocrinol., February 1, 2001; 15(2): 241 - 254. [Abstract] [Full Text]
|
|
|
|
|
|
N. S. Belaguli, J. L. Sepulveda, V. Nigam, F. Charron, M. Nemer, and R. J. Schwartz Cardiac Tissue Enriched Factors Serum Response Factor and GATA-4 Are Mutual Coregulators Mol. Cell. Biol., October 15, 2000; 20(20): 7550 - 7558. [Abstract] [Full Text]
|
|
|
|
|
|
J.-a. Tan, S. H. Hall, P. Petrusz, and F. S. French Thyroid Receptor Activator Molecule, TRAM-1, Is an Androgen Receptor Coactivator Endocrinology, September 1, 2000; 141(9): 3440 - 3450. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
S.-K. Lee, S.-Y. Na, S.-Y. Jung, J.-E. Choi, B. H. Jhun, J. Cheong, P. S. Meltzer, Y. C. Lee, and J. W. Lee Activating Protein-1, Nuclear Factor-{kappa}B, and Serum Response Factor as Novel Target Molecules of the Cancer-Amplified Transcription Coactivator ASC-2 Mol. Endocrinol., June 1, 2000; 14(6): 915 - 925. [Abstract] [Full Text]
|
|
|
|
|
|
S.-K. Lee, J.-H. Kim, Y. C. Lee, J. Cheong, and J. W. Lee Silencing Mediator of Retinoic Acid and Thyroid Hormone Receptors, as a Novel Transcriptional Corepressor Molecule of Activating Protein-1, Nuclear Factor-kappa B, and Serum Response Factor J. Biol. Chem., April 21, 2000; 275(17): 12470 - 12474. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
S.-K. Lee, S. L. Anzick, J.-E. Choi, L. Bubendorf, X.-Y. Guan, Y.-K. Jung, O. P. Kallioniemi, J. Kononen, J. M. Trent, D. Azorsa, et al. A Nuclear Factor, ASC-2, as a Cancer-amplified Transcriptional Coactivator Essential for Ligand-dependent Transactivation by Nuclear Receptors in Vivo J. Biol. Chem., November 26, 1999; 274(48): 34283 - 34293. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
S.-K. Lee, H.-J. Kim, J. W. Kim, and J. W. Lee Steroid Receptor Coactivator-1 and Its Family Members Differentially Regulate Transactivation by the Tumor Suppressor Protein p53 Mol. Endocrinol., November 1, 1999; 13(11): 1924 - 1933. [Abstract] [Full Text]
|
|
|
|
|
|
S.-Y. Na, J.-E. Choi, H.-J. Kim, B. H. Jhun, Y.-C. Lee, and J. W. Lee Bcl3, an Ikappa B Protein, Stimulates Activating Protein-1 Transactivation and Cellular Proliferation J. Biol. Chem., October 1, 1999; 274(40): 28491 - 28496. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
H.-J. Kim, J.-Y. Yi, H.-S. Sung, D. D. Moore, B. H. Jhun, Y. C. Lee, and J. W. Lee Activating Signal Cointegrator 1, a Novel Transcription Coactivator of Nuclear Receptors, and Its Cytosolic Localization under Conditions of Serum Deprivation Mol. Cell. Biol., September 1, 1999; 19(9): 6323 - 6332. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 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]
|
|
|
|
|
|
S.-Y. Na, B. Y. Kang, S. W. Chung, S.-J. Han, X. Ma, G. Trinchieri, S.-Y. Im, J. W. Lee, and T. S. Kim Retinoids Inhibit Interleukin-12 Production in Macrophages through Physical Associations of Retinoid X Receptor and NFkappa B J. Biol. Chem., March 19, 1999; 274(12): 7674 - 7680. [Abstract] [Full Text] [PDF]
|
|
