1 Howard Hughes Medical Institute, Department and School of Medicine, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA 920393-0648, USA
* Author for correspondence (e-mail: mrosenfeld{at}ucsd.edu )
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Summary |
---|
Key words: N-CoR, SMRT, Co-repressor, HDAC
![]() |
Introduction |
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|
![]() |
Identification of nuclear receptor co-repressors |
---|
N-CoR and SMRT both contain a conserved bipartite
nuclear-receptor-interaction domain (NRID)
(Li et al., 1997a;
Seol et al., 1996
;
Zamir et al., 1996
) and three
independent repressor domains that can actively repress a heterologous
DNA-binding domain (Chen and Evans,
1995
; Horlein et al.,
1995
; Ordentlich et al.,
1999
; Park et al.,
1999
) (Fig. 1b).
Further analysis of the NRIDs revealed that each contains a critical
L-X-X-X-I-X-X-X-I/L motif, which includes the L/I-X-X-I/V-I motif termed the
CoRNR box (Hu and Lazar, 1999
;
Nagy et al., 1999
;
Perissi et al., 1999
). This
L-X-X-X-I-X-X-X-I/L motif is similar to the L-X-X-L-L recognition motif
present in nuclear receptor coactivators
(Heery et al., 1997
;
McInerney et al., 1998
) but is
predicted to form an extended
-helix one helical turn longer than the
coactivator motif. A preference of RAR for SMRT and T3R for N-CoR
(Cohen et al., 2000
) is due to
specific sequences in the L-X-X-X-I-X-X-X-I/L motif
(Hu et al., 2001
) as well as
to a T3R-specific interaction domain present in N-CoR but not SMRT
(Cohen et al., 2001
).
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Identification of histone deacetylase proteins |
---|
Rpd3p is linked by epistasis to Sin3p (Rpd1)
(Bowdish and Mitchell, 1993;
McKenzie et al., 1993
;
Vidal and Gaber, 1991
), which
was initially identified in genetic screens for mutations allowing expression
of HO (homothallic gene) in the absence of its activating
protein, Swi5 (Nasmyth et al.,
1987
). Although an enzymatic function of Sin3p has not been
demonstrated, the protein can be linked through the SWI proteins to
chromatin-remodeling events (Winston and
Carlson, 1992
). Sin3p and Rpd3p are both required for full
repression and full activation of transcription of several target genes in
yeast (Vannier et al., 1996
;
Vidal and Gaber, 1991
;
Vidal et al., 1991
), which
suggests that, in common with histone acetylation, histone deacetylation is a
major player in the regulation of transcription.
To address the relationship between histone deacetylation and transcription
at the most basic level, Kadonaga and colleagues used purified recombinant
Drosophila HDAC1 in in vitro transcription assays on chromatinized
templates (Huang and Kadonaga,
2001). Their experiments demonstrate that HDAC1 alone can mediate
histone deacetylation and that a Gal4-dHDAC1 fusion protein can repress
transcription by
60% on chromatinized templates but not on naked DNA
templates. Their data also suggest that HDAC activity blocks the initiation
step of transcription. In some systems, N-CoR and SMRT can function as
activating cofactors of HDAC3 (Guenther et
al., 2001
; Wen et al.,
2000
). This activation of HDAC3 is mediated by a domain of N-CoR
and SMRT that overlaps with the SANT domain (named for its presence in
Swi3, Ada2, N-CoR, and TFIIB)
(Aasland et al., 1996
;
Wen et al., 2000
;
Guenther et al., 2001
).
In addition to the class I and class II HDAC families, which are themselves
related, a distinct class of HDAC proteins (class III HDACs) exists: silent
information regulator 2 (SIR2)-like proteins
(Gottschling, 2000). The
SIR2 genes were initially identified by analysis of mutations that
result in expression of regions of the yeast genome that are normally
transcriptionally silenced (Nasmyth,
1982
; Rine et al.,
1979
). Indeed, Braunstein et al., prior to the identification of
the class I and class II HDAC proteins, noted that overexpression of Sir2p in
yeast cells produces histones that are under acetylated
(Braunstein et al., 1993
).
This suggested, although in the absence of any biochemical evidence, that
Sir2p has a role in histone deacetylation. Later studies identified
nicotinamide adenine dinucleotide (NAD)-dependent ADP-ribosyltransferase
activity associated with the human Sir2p homologue
(Tsang and Escalante-Semerena,
1998
), and extension of these studies revealed the surprising fact
that Sir2p is in fact an NAD-dependent histone deacetylase
(Imai et al., 2000
;
Landry et al., 2000
;
Smith et al., 2000
).
Interestingly, mammalian Sir2 can interact with and deacetylate the p53
protein, reducing the transcriptional activity of p53
(Luo et al., 2001
;
Vaziri et al., 2001
). The
potential ability of this and other classes of HDACs to deacetylate proteins
other than histones raises interesting possibilities for their ability to
regulate gene expression.
The precise roles of histone deacetylation in transcriptional repression
are not fully understood. For instance, differential display analysis of cells
treated with the histone deacetylase inhibitor trichostatin A (TSA) revealed
that the expression of just 2% of cellular genes (8 of 340 genes examined)
changed, despite an increase in core histone acetylation
(Van Lint et al., 1996).
Rpd3p-null strains in yeast have defects in both transcriptional repression
and activation (Rundlett et al.,
1996
; Vidal et al.,
1991
) and in fact show increased repression at telomeric
heterochromatin (Rundlett et al.,
1996
), revealing the complicated nature of the transcriptional
alterations produced by promoter-specific usage of co-regulatory factors.
Recent studies examining the acetylation state at various promoters revealed
that different transcriptional activators confer distinct patterns of histone
acetylation and that activation is not necessarily related to increased
acetylation (Deckert and Struhl,
2001
). Experiments with Sin3p and Rpd3 mutants, however, did
reveal decreased acetylation of histones
(Deckert and Struhl, 2001
).
Thus many questions relating to the complex nature of transcriptional
repression versus activation with regards to the acetylation state of histones
remain, although the finding that the class III HDAC Sir2 can deacetylate p53
(Luo et al., 2001
;
Vaziri et al., 2001
) suggests
that HDAC proteins have multiple roles in the cell.
![]() |
Purification of co-repressor complexes |
---|
|
Depending on the purification strategy, different HDAC proteins, including
HDAC1, HDAC2 and HDAC3, have also been identified in both N-CoR and SMRT
complexes (Fig. 1b)
(Guenther, 2000;
Jones et al., 2001
;
Li et al., 2000
;
Underhill et al., 2000
;
Wen et al., 2000
). A subset
of N-CoR complexes share common components with the SAP complex and contain
HDAC1, HDAC2 and mSin3 (Zhang et al.,
1997
; Zhang et al.,
1998c
). Biochemical purification of complexes using anti-N-CoR or
anti-HDAC3 antibodies also revealed a distinct complex that contains HDAC3,
N-CoR or SMRT, and transducin (beta)-like
protein 1(TBL1) (Fig.
1b) (Guenther et al.,
2000
; Li et al.,
2000
; Underhill et al.,
2000
; Wen et al.,
2000
). TBL-1 has six WD-40 repeats
(Bassi et al., 1999
), a motif
also present in the Tup1 and Groucho corepressors, and is homologous to the
Drosophila protein ebi, which is involved in epidermal growth factor
receptor signaling pathways (Dong et al.,
1999
). Under different conditions, an N-CoRSMRTHDAC3
complex can also contain Krab-associated
protein 1 (KAP-1), a TSA-sensitive co-repressor that interacts with
members of the heterochromatin protein 1 (HP1) family, and several members of
the Swi/Snf ATP-dependent chromatin-remodeling complex family, which is
reminiscent of the ATP-dependent chromatin-remodeling proteins found in the
NURD complex (Fig. 1b;
Fig. 2)
(Underhill et al., 2000
).
Several groups have also shown that the third repressor domain of N-CoR and
SMRT can directly interact in vitro with class II HDACs, including HDAC4,
HDAC5 and HDAC7 (Huang et al.,
2000
; Kao et al.,
2000
), suggesting the full range of complexes has yet to be
purified.
HDAC1 and HDAC2 have also been identified as part of a complex containing
CoREST and a novel protein homologous to a diverse group of oxidases and
dehydrogenases (Fig. 2)
(Humphrey et al., 2001;
You et al., 2001
), which is
also present in one version of the NURD complex
(Tong et al., 1998
). This
latter protein is of particular interest because its potential enzymatic
function is reminiscent not only of the NAD-dependent Sir proteins discussed
earlier but of another family of co-repressor proteins, the C-terminal binding
proteins (CtBP), which have homology to dehydrogenase enzymes
(Nibu et al., 1998
;
Schaeper et al., 1998
). This
suggests yet another enzymatic activity may be involved in transcriptional
repression. Note that CoREST, which was first identified as a co-repressor for
the neural restrictive factor REST (Andres
et al., 1999
), MTA1, a component of the NURD complex, and N-CoR
and SMRT each contains a SANT domain
(Aasland et al., 1996
). This
suggests that this domain is important for some aspects of repression.
![]() |
Other transcription factor partners |
---|
N-CoR and SMRT have also been implicated as co-repressors for a variety of
unrelated transcription factors, which regulate diverse cellular processes
(Fig. 1b). SMRT interacts with
and can repress transcription by serum response factor (SRF), activator
protein-1 (AP-1) and nuclear factor-B (NF
B), which are all
transcription factors involved in stimulation of cell proliferation
(Lee et al., 2000
). N-CoR and
SMRT have both been implicated in abrogation of transcription by the
evolutionarily related POU homeodomain factors Pit-1
(Xu et al., 1998
) and Oct-1
(Kakizawa et al., 2001
), which
have important developmental roles, and by the homeobox factor PBX
(Asahara et al., 1999
;
Shanmugam et al., 1999
),
which is an important determiner of cell fate and segment identity. These
co-repressors also interact with the Poz/zinc finger transcription factor
BCL-6, which may influence apoptosis
(Dhordain et al., 1998
;
Huynh and Bardwell, 1998
;
Wong and Privalsky, 1998
),
and with the bHLH proteins MAD (Heinzel et
al., 1997
), MyoD (Bailey et
al., 1999
) and HES-related repressor proteins (HERPs)
(Iso et al., 2001
), to
suppress proliferation or induce terminal differentiation, as well as with the
Notch-activated adapter protein Su(H)/RBP-J/CBF1
(Kao et al., 1998
), which
influences differentiation, proliferation and apoptosis in many developmental
systems. SMRT has most recently been shown to interact with signal transducers
and activators of transcription 5 (STAT5)
(Nakajima et al., 2001
), which
plays a central role in cytokine signaling.
![]() |
Multiple mechanisms of regulation |
---|
Although association of N-CoR and SMRT with nuclear receptors is clearly
controlled at the level of hormone binding, in several systems, cell signaling
events seem capable of directly regulating the association of nuclear
receptors with N-CoR and SMRT. Treatment of treated MCF-7 or Hela cells with
forskolin, which stimulates the PKA pathway, or EGF, which stimulates the ERK
MAP kinase and PKC pathways, resulted in decreased association of N-CoR with
ER in the presence of the antagonist tamoxifen
(Lavinsky et al., 1998). In
addition, in microinjection assays, treatment with forskolin or EGF converts
tamoxifen from an antagonist to an agonist of ER-mediated transcription
(Lavinsky et al., 1998
).
Activation of the ERK MAP kinase pathway by L-throxine (T4) results
in serine phosphorylation of TRß1 and dissociation of SMRT in a
hormone-independent manner (Davis et al.,
2000
). Similarly, phosphorylation of SMRT by the MAP kinase kinase
MEK-1 and MEK-1 kinase (MEKK-1) can inhibit interactions between SMRT and
nuclear receptors or PLZF (Hong and
Privalsky, 2000
). In contrast, phosphorylation of SMRT by casein
kinase II (CK2) stabilizes the SMRTnuclear-receptor interaction
(Zhou et al., 2001
). Thus,
different cell signaling pathways can effect different transcriptional
outcomes.
In addition to their role in modulating protein-protein interactions, cell
signaling pathways also cause changes in subcellular distribution, presumably
to restrict access of transcription factors to co-repressors. CamKIV
phosphorylation of the NFB p65 subunit results not only in an exchange
of SMRT for CBP but also in translocation of SMRT to the cytoplasm
(Jang et al., 2001
). MEK-1 and
MEKK-1 signaling produces a redistribution of SMRT from the nucleus to the
perinucleus or cytoplasm (Hong and
Privalsky, 2000
). Interestingly, co-repressors themselves shuttle
associated proteins to the nucleus, as is the case for both Su(H)/RBP-J/CBF1
(Zhou and Hayward, 2001
) and
certain HDAC proteins (Wu et al.,
2001
). Intracellular signaling events are also thought to
influence the subcellular distribution of HDAC proteins
(Grozinger and Schreiber,
2000
; McKinsey et al.,
2000a
; McKinsey et al.,
2000b
) and thus may be a general mechanism by which co-repressor
proteins are regulated.
There are also examples of regulation of co-repressor specificity by its
association with other co-repressor molecules to form distinct co-repressor
complexes. Members of the Ski proto-oncogene family, which includes the
proteins Ski and Sno, form complexes with N-CoR, SMRT, HDACs and mSin3 to
regulate transcriptional repression by MAD and TRß
(Nomura et al., 1999). A
co-repressor complex containing N-CoR and Ski or Sno has also been implicated
as a negative regulator of the TGFß signaling pathway
(Luo et al., 1999
;
Stroschein et al., 1999
). Ski
or Sno, together with N-CoR, form complexes with the SMAD proteins that
positively regulate TGFß signaling
(Moustakas et al., 2001
),
repressing TGFß-activated transcription
(Luo et al., 1999
;
Stroschein et al., 1999
).
SMRT also interacts with the transcriptional repressor SMRT/HDAC1
associated repressor protein (SHARP) (Shi
et al., 2001). Interestingly, SHARP binds the steroid receptor RNA
coactivator SRA and suppresses SRA-activated steroid receptor transcription
activity, providing a mechanism by which SMRT can modulate liganded nuclear
receptors (Shi et al., 2001
).
As the data collected increase, there will doubtlessly prove to be additional
mechanisms by which both the regulation and specificity of N-CoR and SMRT
activity are controlled.
![]() |
Roles in development and disease |
---|
A dominant-negative N-CoR protein, lacking the repression domains in the
N-terminus but retaining the nuclear receptor interaction domains, has also
been used in an attempt to define specific biological roles for co-repressors
(Feng et al., 2001).
Transgenic mice expressing this construct in hepatocytes showed an increased
proliferation of hepatocytes and a derepression of T3-regulated hepatic target
genes (Feng et al., 2001
). A
dominant-negative approach has also been used in Xenopus and resulted
in embryos that exhibited phenotypes similar to those treated by RA, namely
reduction of anterior structures such as forebrain and cement gland
(Koide et al., 2001
). These
data suggest that RAR-mediated repression of target genes is critical for head
formation.
Whereas knockout and dominant-negative transgenic animals allow one to
assess the consequences of loss of co-repressor function, various disease
models have allowed investigation of inappropriate gain of co-repressor
function (Table 1). For
instance, resistance to thyroid hormone (RTH) is a human genetic disease
characterized by an impaired physiological response to thyroid hormone and is
associated with mutations in T3R-ß
(Kopp et al., 1996) that fail
to release N-CoR or SMRT upon hormone treatment
(Safer et al., 1998
;
Yoh et al., 1997
).
Transcriptional activation by mutant T3R-ß in response to
hormone is diminished compared with that of wild-type T3R-ß.
Repression might also be involved in normal thyroid hormone physiology because
deletion of genes encoding all known thyroid hormone receptors results in a
phenotype less severe than that of mice lacking thyroid hormone
(Gothe et al., 1999
). Thus,
there seems to be a role for the unliganded T3Rs in development,
which suggests co-repressor involvement.
|
Roles for N-CoR and SMRT in several types of leukemia are also well
characterized. Acute promyelocytic leukemia (APL), caused by a block in
myeloid differentiation, is associated with rearrangements of
RAR-, which most commonly result in fusions of the
RAR-
gene with the promyelocytic leukemia gene (PML)
or the promyelocytic leukemia zinc finger gene (PLZF)
(Lin et al., 1999
). Both
RAR-
fusion proteins retain the ability to interact with N-CoR and SMRT
(Hong et al., 1997
).
Interestingly, although retinoic acid (RA) can induce remission in APLs
resulting from PML-RAR-
translocations, APLs resulting from
PLZF-RAR-
translocations are insensitive to RA
(Lin et al., 1999
). Although
co-repressor interactions with PML-RAR-
fusions are less sensitive to
the effects of RA than are interactions with wild-type RAR-
,
pharmacological concentrations of RA do result in the dismissal of the
co-repressor complex and in activation of transcription. In contrast, the
PLZF-RAR-
fusion protein interacts with the co-repressor even in the
presence of RA. These observations correlate co-repressors with the disease
state, because the relative RA sensitivity of the interaction between the
RAR-
fusions and N-CoR or SMRT correlates with their response to RA
treatment. Interestingly, histone deacetylase inhibitors such as TSA, in
combination with RA, not only overcome the transcriptional repressor activity
of both PML-RAR-
and PLZF-RAR-
but also render PLZF-RAR-
sensitive to RA (He et al.,
1998
). Together, these results indicate that the presence of a
co-repressor is one criterion for disease progression.
N-CoR and SMRT have also been implicated in acute myeloid leukemias (AML).
12-15% of AMLs result from the t(8;21) translocation between AML1 and
ETO. AML1 upregulates a number of target genes critical to normal
hematopoiesis, and the AML1-ETO fusion protein represses transcription of
these target genes. In common with ETO, the AML1-ETO fusion protein can
interact with N-CoR and SMRT, and mutations that abolish this interaction
affect the ability of AML1-ETO both to repress transcription and to inhibit
differentiation of hematopoeitic precursors
(Gelmetti et al., 1998;
Lutterbach et al., 1998
;
Wang et al., 1998
). The role
of N-CoR in AML also appears to be partially due to recruitment of histone
deacetylase activity, since recent studies have revealed that the histone
deacetylase inhibitors TSA and phenylbutyrate (PB) both partially reverse
ETO-mediated transcriptional repression, and PB can induce partial
differentiation of an AML1-ETO cell line
(Wang et al., 1999
).
A third class of leukemia results from chromosomal rearrangements of the
E26 transforming specific (ETS)-related gene TEL, which encodes a
strong transcriptional repressor that recruits a co-repressor complex
including SMRT, mSin3A and HDAC3
(Chakrabarti and Nucifora,
1999; Wang and Hiebert,
2001
). The overall theme for involvement of N-CoR and SMRT in
progression of these leukemias thus appears to be the ability of
histone-deacetylase-associated repression to block differentiation and allow
uncontrolled growth of hematopoietic cells, which ultimately results in the
diseased state.
N-CoR has also been implicated in pathologies associated with the nervous
system. The C-terminus of N-CoR interacts with the N-terminus of the
Huntington's disease gene product, huntingtin, in both yeast two-hybrid
screens and pull-down assays (Boutell et
al., 1999). Although N-CoR is generally thought to exert its
action in the nucleus (Horlein et al.,
1995
), immunohistochemical studies on Huntington's disease brains
and control brains revealed that the localization of N-CoR and mSin3 in the
diseased cortex and caudate is exclusively cytoplasmic, whereas in the normal
brain they are localized in the nucleus as well as the cytoplasm. This
suggests that relocalization of co-repressor proteins in the diseased brain
alters transcription and is thus involved in the pathology of this disease.
Interestingly, though perhaps counter-intuitively, inhibitors of HDAC activity
can arrest neurodegeneration associated with Huntington's disease in a
Drosophila model (Steffan et
al., 2001
).
![]() |
Conclusions |
---|
It is intriguing, as mentioned earlier, that a growing number of
co-repressor complexes are associated, if circumstantially, with proteins
connected to redox pathways. These include CTBP, the FAD-binding protein found
in the HDAC1/2 and NURD complexes, and the NAD-dependent class 3 HDACs.
Several lines of evidence also point to a connection between DNA methylation
and histone deacetylation (Dobosy and
Selker, 2001), suggesting that multiple enzymatic activities are
recruited to DNA, either simultaneously or sequentially, and subsequently
modulate transcriptional repression.
![]() |
Acknowledgments |
---|
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References |
---|
Aasland, R., Stewart, A. F. and Gibson, T. (1996). The SANT domain: a putative DNA-binding domain in the SWI-SNF and ADA complexes, the transcriptional co-repressor N-CoR and TFIIIB. Trends Biochem. Sci. 21,87 -88.[Medline]
Andres, M. E., Burger, C., Peral-Rubio, M. J., Battaglioli, E.,
Anderson, M. E., Grimes, J., Dallman, J., Ballas, N. and Mandel, G.
(1999). CoREST: a functional co-repressor required for regulation
of neural-specific gene expression. Proc. Natl. Acad. Sci.
USA 96,9873
-9878.
Asahara, H., Dutta, S., Kao, H. Y., Evans, R. M. and Montminy,
M. (1999). Pbx-Hox heterodimers recruit
coactivator-co-repressor complexes in an isoform-specific manner.
Mol. Cell. Biol. 19,8219
-8225.
Bailey, P., Downes, M., Lau, P., Harris, J., Chen, S. L.,
Hamamori, Y., Sartorelli, V. and Muscat, G. E. (1999). The
nuclear receptor co-repressor N-CoR regulates differentiation: N-CoR directly
interacts with MyoD. Mol. Endocrinol.
13,1155
-1168.
Baniahmad, A., Kohne, A. C. and Renkawitz, R. (1992). A transferable silencing domain is present in the thyroid hormone receptor, in the v-erbA oncogene product and in the retinoic acid receptor. EMBO J. 11,1015 -1023.[Abstract]
Bassi, M. T., Ramesar, R. S., Caciotti, B., Winship, I. M., De Grandi, A., Riboni, M., Townes, P. L., Beighton, P., Ballabio, A. and Borsani, G. (1999). X-linked late-onset sensorineural deafness caused by a deletion involving OA1 and a novel gene containing WD-40 repeats. Am. J. Hum. Genet. 64,1604 -1616.[Medline]
Bauer, A., Mikulits, W., Lagger, G., Stengl, G., Brosch, G. and
Beug, H. (1998). The thyroid hormone receptor functions as a
ligand-operated developmental switch between proliferation and differentiation
of erythroid progenitors. EMBO J.
17,4291
-4303.
Boutell, J. M., Thomas, P., Neal, J. W., Weston, V. J., Duce,
J., Harper, P. S. and Jones, A. L. (1999). Aberrant
interactions of transcriptional repressor proteins with the Huntington's
disease gene product, huntingtin. Hum. Mol. Genet.
8,1647
-1655.
Bowdish, K. S. and Mitchell, A. P. (1993). Bipartite structure of an early meiotic upstream activation sequence from Saccharomyces cerevisiae. Mol. Cell. Biol. 13,2172 -2181.[Abstract]
Braunstein, M., Rose, A. B., Holmes, S. G., Allis, C. D. and Broach, J. R. (1993). Transcriptional silencing in yeast is associated with reduced nucleosome acetylation. Genes Dev. 7,592 -604.[Abstract]
Busch, K., Martin, B., Baniahmad, A., Martial, J. A., Renkawitz,
R. and Muller, M. (2000). Silencing subdomains of v-ErbA
interact cooperatively with co-repressors: involvement of helices 5/6.
Mol. Endocrinol. 14,201
-211.
Chakrabarti, S. R. and Nucifora, G. (1999). The leukemia-associated gene TEL encodes a transcription repressor which associates with SMRT and mSin3A. Biochem. Biophys. Res. Commun. 264,871 -877.[Medline]
Chen, G. and Courey, A. J. (2000). Groucho/TLE family proteins and transcriptional repression. Gene 249, 1-16.[Medline]
Chen, J. D. and Evans, R. M. (1995). A transcriptional co-repressor that interacts with nuclear hormone receptors. Nature 377,454 -457.[Medline]
Ciana, P., Braliou, G. G., Demay, F. G., von Lindern, M.,
Barettino, D., Beug, H. and Stunnenberg, H. G. (1998).
Leukemic transformation by the v-ErbA oncoprotein entails constitutive binding
to and repression of an erythroid enhancer in vivo. EMBO
J. 17,7382
-7394.
Cohen, R. N., Putney, A., Wondisford, F. E. and Hollenberg, A.
N. (2000). The nuclear co-repressors recognize distinct
nuclear receptor complexes. Mol. Endocrinol.
14,900
-914.
Cohen, R. N., Brzostek, S., Kim, B., Chorev, M., Wondisford, F.
E. and Hollenberg, A. N. (2001). The specificity of
interactions between nuclear hormone receptors and co-repressors is mediated
by distinct amino acid sequences within the interacting domains.
Mol. Endocrinol. 15,1049
-1061.
Crawford, P. A., Dorn, C., Sadovsky, Y. and Milbrandt, J.
(1998). Nuclear receptor DAX-1 recruits nuclear receptor
co-repressor N-CoR to steroidogenic factor 1. Mol. Cell.
Biol. 18,2949
-2956.
Damm, K., Thompson, C. C. and Evans, R. M. (1989). Protein encoded by v-erbA functions as a thyroid-hormone receptor antagonist. Nature 339,593 -597.[Medline]
Dasen, J. S., Barbera, J. P., Herman, T. S., Connell, S. O.,
Olson, L., Ju, B., Tollkuhn, J., Baek, S. H., Rose, D. W. and Rosenfeld, M.
G. (2001) Temporal regulation of a paired-like homeodomain
repressor/TLE corepressor complex and a related activator is required for
pituitary organogenesis. Genes Dev.
15,3193
-3207.
Davis, P. J., Shih, A., Lin, H. Y., Martino, L. J. and Davis, F.
B. (2000). Thyroxine promotes association of
mitogen-activated protein kinase and nuclear thyroid hormone receptor (TR) and
causes serine phosphorylation of TR. J. Biol. Chem.
275,38032
-38039.
Deckert, J. and Struhl, K. (2001). Histone
acetylation at promoters is differentially affected by specific activators and
repressors. Mol. Cell Biol.
21,2726
-2735.
Dhordain, P., Lin, R. J., Quief, S., Lantoine, D., Kerckaert, J.
P., Evans, R. M. and Albagli, O. (1998). The LAZ3(BCL-6)
oncoprotein recruits a SMRT/mSIN3A/histone deacetylase containing complex to
mediate transcriptional repression. Nucleic Acids Res.
26,4645
-4651.
Dobosy, J. R. and Selker, E. U. (2001). Emerging connections between DNA methylation and histone acetylation. Cell. Mol. Life Sci. 58,721 -727.[Medline]
Dong, X., Tsuda, L., Zavitz, K. H., Lin, M., Li, S., Carthew, R.
W. and Zipursky, S. L. (1999). ebi regulates epidermal growth
factor receptor signaling pathways in Drosophila. Genes
Dev. 13,954
-965.
Dowell, P., Ishmael, J. E., Avram, D., Peterson, V. J., Nevrivy,
D. J. and Leid, M. (1999). Identification of nuclear receptor
co-repressor as a peroxisome proliferator-activated receptor alpha interacting
protein. J. Biol. Chem.
274,15901
-15907.
Feng, X., Jiang, Y., Meltzer, P. and Yen, P. M.
(2001). Transgenic targeting of a dominant negative co-repressor
to liver blocks basal repression by thyroid hormone receptor and increases
cell proliferation. J. Biol. Chem.
276,15066
-15072.
Gelmetti, V., Zhang, J., Fanelli, M., Minucci, S., Pelicci, P.
G. and Lazar, M. A. (1998). Aberrant recruitment of the
nuclear receptor co-repressor-histone deacetylase complex by the acute myeloid
leukemia fusion partner ETO. Mol. Cell. Biol.
18,7185
-7191.
Gothe, S., Wang, Z., Ng, L., Kindblom, J. M., Barros, A. C.,
Ohlsson, C., Vennstrom, B. and Forrest, D. (1999). Mice
devoid of all known thyroid hormone receptors are viable but exhibit disorders
of the pituitary-thyroid axis, growth, and bone maturation. Genes
Dev. 13,1329
-1341.
Gottschling, D. E. (2000). Gene silencing: two faces of SIR2. Curr. Biol. 10,R708 -R711.[Medline]
Graf, T. and Beug, H. (1983). Role of the v-erbA and v-erbB oncogenes of avian erythroblastosis virus in erythroid cell transformation. Cell 34,7 -9.[Medline]
Gray, S. G. and Ekstrom, T. J. (2001). The human histone deacetylase family. Exp. Cell Res. 262, 75-83.[Medline]
Grozinger, C. M. and Schreiber, S. L. (2000).
Regulation of histone deacetylase 4 and 5 and transcriptional activity by
14-3-3-dependent cellular localization. Proc. Natl. Acad. Sci.
USA 97,7835
-7840.
Grunstein, M. (1990). Histone function in transcription. Annu. Rev. Cell Biol. 6, 643-678.
Guenther, M. G., Lane, W. S., Fischle, W., Verdin, E., Lazar, M.
A. and Shiekhattar, R. (2000). A core SMRT co-repressor
complex containing HDAC3 and TBL1, a WD40- repeat protein linked to deafness.
Genes Dev. 14,1048
-1057.
Guenther, M. G., Barak, O. and Lazar, M. A.
(2001). The smrt and n-cor co-repressors are activating cofactors
for histone deacetylase 3. Mol. Cell Biol.
21,6091
-6101.
He, L. Z., Guidez, F., Tribioli, C., Peruzzi, D., Ruthardt, M., Zelent, A. and Pandolfi, P. P. (1998). Distinct interactions of PML-RARalpha and PLZF-RARalpha with co- repressors determine differential responses to RA in APL. Nat. Genet. 18,126 -135.[Medline]
Heery, D. M., Kalkhoven, E., Hoare, S. and Parker, M. G. (1997). A signature motif in transcriptional co-activators mediates binding to nuclear receptors. Nature 387,733 -736.[Medline]
Heinzel, T., Lavinsky, R. M., Mullen, T. M., Soderstrom, M., Laherty, C. D., Torchia, J., Yang, W. M., Brard, G., Ngo, S. D., Davie, J. R. et al. (1997). A complex containing N-CoR, mSin3 and histone deacetylase mediates transcriptional repression. Nature 387,43 -48.[Medline]
Hong, S. H., David, G., Wong, C. W., Dejean, A. and Privalsky,
M. L. (1997). SMRT co-repressor interacts with PLZF and with
the PML-retinoic acid receptor alpha (RARalpha) and PLZF-RARalpha oncoproteins
associated with acute promyelocytic leukemia. Proc. Natl. Acad.
Sci. USA 94,9028
-9033.
Hong, S. H. and Privalsky, M. L. (2000). The
SMRT co-repressor is regulated by a MEK-1 kinase pathway: inhibition of
co-repressor function is associated with SMRT phosphorylation and nuclear
export. Mol. Cell. Biol.
20,6612
-6625.
Horlein, A. J., Naar, A. M., Heinzel, T., Torchia, J., Gloss, B., Kurokawa, R., Ryan, A., Kamei, Y., Soderstrom, M., Glass, C. K. et al. (1995). Ligand-independent repression by the thyroid hormone receptor mediated by a nuclear receptor co-repressor. Nature 377,397 -404.[Medline]
Hu, G., Chung, Y. L., Glover, T., Valentine, V., Look, A. T. and Fearon, E. R. (1997). Characterization of human homologs of the Drosophila seven in absentia (sina) gene. Genomics 46,103 -111.[Medline]
Hu, X. and Lazar, M. A. (1999). The CoRNR motif controls the recruitment of co-repressors by nuclear hormone receptors. Nature 402,93 -96.[Medline]
Hu, X., Li, Y. and Lazar, M. A. (2001).
Determinants of CoRNR-dependent repression complex assembly on nuclear hormone
receptors. Mol. Cell. Biol.
21,1747
-1758.
Huang, E. Y., Zhang, J., Miska, E. A., Guenther, M. G.,
Kouzarides, T. and Lazar, M. A. (2000). Nuclear receptor
co-repressors partner with class II histone deacetylases in a Sin3-independent
repression pathway. Genes Dev.
14, 45-54.
Huang, X. and Kadonaga, J. T. (2001).
Biochemical analysis of transcriptional repression by Drosophila histone
deacetylase 1. J. Biol. Chem.
276,12497
-12500.
Humphrey, G. W., Wang, Y., Russanova, V. R., Hirai, T., Qin, J.,
Nakatani, Y. and Howard, B. H. (2001). Stable histone
deacetylase complexes distinguished by the presence of SANT domain proteins
CoREST/kiaa0071 and Mta-L1. J. Biol. Chem.
276,6817
-6824.
Huynh, K. D. and Bardwell, V. J. (1998). The BCL-6 POZ domain and other POZ domains interact with the co- repressors N-CoR and SMRT. Oncogene 17,2473 -2484.[Medline]
Imai, S., Armstrong, C. M., Kaeberlein, M. and Guarente, L. (2000). Transcriptional silencing and longevity protein Sir2 is an NAD- dependent histone deacetylase. Nature 403,795 -800.[Medline]
Iso, T., Sartorelli, V., Poizat, C., Iezzi, S., Wu, H. Y.,
Chung, G., Kedes, L. and Hamamori, Y. (2001). Herp, a novel
heterodimer partner of hes/e(spl) in notch signaling. Mol. Cell.
Biol. 21,6080
-6089.
Jackson, T. A., Richer, J. K., Bain, D. L., Takimoto, G. S.,
Tung, L. and Horwitz, K. B. (1997). The partial agonist
activity of antagonist-occupied steroid receptors is controlled by a novel
hinge domain-binding coactivator L7/SPA and the co-repressors N-CoR or SMRT.
Mol. Endocrinol. 11,693
-705.
Jang, M. K., Goo, Y. H., Sohn, Y. C., Kim, Y. S., Lee, S. K.,
Kang, H., Cheong, J. and Lee, J. W. (2001).
Ca2+/calmodulin-dependent protein kinase IV stimulates nuclear
factor- kappa B transactivation via phosphorylation of the p65 subunit.
J. Biol. Chem. 276,20005
-20010.
Jepsen, K., Hermanson, O., Onami, T. M., Gleiberman, A. S., Lunyak, V., McEvilly, R. J., Kurokawa, R., Kumar, V., Liu, F., Seto, E. et al. (2000). Combinatorial roles of the nuclear receptor co-repressor in transcription and development. Cell 102,753 -763.[Medline]
Jones, P. L., Veenstra, G. J., Wade, P. A., Vermaak, D., Kass, S. U., Landsberger, N., Strouboulis, J. and Wolffe, A. P. (1998). Methylated DNA and MeCP2 recruit histone deacetylase to repress transcription. Nat. Genet. 19,187 -191.[Medline]
Jones, P. L., Sachs, L. M., Rouse, N., Wade, P. A. and Shi, Y.
B. (2001). Multiple N-CoR complexes contain distinct histone
deacetylases. J. Biol. Chem.
276,8807
-8811.
Kakizawa, T., Miyamoto, T., Ichikawa, K., Takeda, T., Suzuki,
S., Mori, J., Kumagai, M., Yamashita, K. and Hashizume, K.
(2001). Silencing mediator for retinoid and thyroid hormone
receptors interacts with octamer transcription factor-1 and acts as a
transcriptional repressor. J. Biol. Chem.
276,9720
-9725.
Kao, H. Y., Ordentlich, P., Koyano-Nakagawa, N., Tang, Z.,
Downes, M., Kintner, C. R., Evans, R. M. and Kadesch, T.
(1998). A histone deacetylase co-repressor complex regulates the
Notch signal transduction pathway. Genes Dev.
12,2269
-2277.
Kao, H. Y., Downes, M., Ordentlich, P. and Evans, R. M.
(2000). Isolation of a novel histone deacetylase reveals that
class I and class II deacetylases promote SMRT-mediated repression.
Genes Dev. 14,55
-66.
Knoepfler, P. S. and Eisenman, R. N. (1999). Sin meets NuRD and other tails of repression. Cell 99,447 -450.[Medline]
Koide, T., Downes, M., Chandraratna, R. A., Blumberg, B. and
Umesono, K. (2001). Active repression of RAR signaling is
required for head formation. Genes Dev.
15,2111
-2121.
Kokura, K., Kaul, S. C., Wadhwa, R., Nomura, T., Khan, M. M.,
Shinagawa, T., Yasukawa, T., Colmenares, C. and Ishii, S.
(2001). The Ski Protein Family Is Required for MeCP2-mediated
Transcriptional Repression. J. Biol. Chem.
276,34115
-34121.
Kopp, P., Kitajima, K. and Jameson, J. L. (1996). Syndrome of resistance to thyroid hormone: insights into thyroid hormone action. Proc. Soc. Exp. Biol. Med. 211, 49-61.[Abstract]
Landry, J., Sutton, A., Tafrov, S. T., Heller, R. C., Stebbins,
J., Pillus, L. and Sternglanz, R. (2000). The silencing
protein SIR2 and its homologs are NAD-dependent protein deacetylases.
Proc. Natl. Acad. Sci. USA
97,5807
-5811.
Lavinsky, R. M., Jepsen, K., Heinzel, T., Torchia, J., Mullen,
T. M., Schiff, R., Del-Rio, A. L., Ricote, M., Ngo, S., Gemsch, J. et al.
(1998). Diverse signaling pathways modulate nuclear receptor
recruitment of N- CoR and SMRT complexes. Proc. Natl. Acad. Sci.
USA 95,2920
-2925.
Lee, S. K., Kim, J. H., Lee, Y. C., Cheong, J. and Lee, J.
W. (2000). Silencing mediator of retinoic acid and thyroid
hormone receptors, as a novel transcriptional co-repressor molecule of
activating protein-1, nuclear factor-kappaB, and serum response factor.
J. Biol. Chem. 275,12470
-12474.
Li, H., Leo, C., Schroen, D. J. and Chen, J. D.
(1997a). Characterization of receptor interaction and
transcriptional repression by the co-repressor SMRT. Mol.
Endocrinol. 11,2025
-2037.
Li, S., Li, Y., Carthew, R. W. and Lai, Z. C. (1997b). Photoreceptor cell differentiation requires regulated proteolysis of the transcriptional repressor Tramtrack. Cell 90,469 -478.[Medline]
Li, J., Wang, J., Nawaz, Z., Liu, J. M., Qin, J. and Wong,
J. (2000). Both co-repressor proteins SMRT and N-CoR exist in
large protein complexes containing HDAC3. EMBO J.
19,4342
-4350.
Lin, R. J., Egan, D. A. and Evans, R. M. (1999). Molecular genetics of acute promyelocytic leukemia. Trends Genet. 15,179 -184.[Medline]
Lu, J., McKinsey, T. A., Nicol, R. L. and Olson, E. N.
(2000). Signal-dependent activation of the MEF2 transcription
factor by dissociation from histone deacetylases. Proc. Natl. Acad.
Sci. USA 97,4070
-4075.
Luo, K., Stroschein, S. L., Wang, W., Chen, D., Martens, E.,
Zhou, S. and Zhou, Q. (1999). The Ski oncoprotein interacts
with the Smad proteins to repress TGFbeta signaling. Genes
Dev. 13,2196
-2206.
Luo, J., Nikolaev, A. Y., Imai, S. I., Chen, D., Su, F., Shiloh, A., Guarente, L. and Gu, W. (2001). Negative control of p53 by Sir2 promotes cell survival under stress. Cell 107,137 -148.[Medline]
Lutterbach, B., Westendorf, J. J., Linggi, B., Patten, A.,
Moniwa, M., Davie, J. R., Huynh, K. D., Bardwell, V. J., Lavinsky, R. M.,
Rosenfeld, M. G. et al. (1998). ETO, a target of t(8;21) in
acute leukemia, interacts with the N-CoR and mSin3 co-repressors.
Mol. Cell. Biol. 18,7176
-7184.
McInerney, E. M., Rose, D. W., Flynn, S. E., Westin, S., Mullen,
T. M., Krones, A., Inostroza, J., Torchia, J., Nolte, R. T., Assa-Munt, N. et
al. (1998). Determinants of coactivator LXXLL motif
specificity in nuclear receptor transcriptional activation. Genes
Dev. 12,3357
-3368.
McKenzie, E. A., Kent, N. A., Dowell, S. J., Moreno, F., Bird, L. E. and Mellor, J. (1993). The centromere and promoter factor, 1, CPF1, of Saccharomyces cerevisiae modulates gene activity through a family of factors including SPT21, RPD1 (SIN3), hdac and and CCR4. Mol. Gen. Genet. 240,374 -386.[Medline]
McKinsey, T. A., Zhang, C. L., Lu, J. and Olson, E. N. (2000a). Signal-dependent nuclear export of a histone deacetylase regulates muscle differentiation. Nature 408,106 -111.[Medline]
McKinsey, T. A., Zhang, C. L. and Olson, E. N.
(2000b). Activation of the myocyte enhancer factor-2
transcription factor by calcium/calmodulin-dependent protein kinase-stimulated
binding of 14-3- 3 to histone deacetylase 5. Proc. Natl. Acad. Sci.
USA 97,14400
-14405.
Moustakas, A., Souchelnytskyi, S. and Heldin, C. H.
(2001). Smad regulation in TGF-ß signal transduction.
J. Cell Sci. 114,4359
-4369.
Munoz, A., Zenke, M., Gehring, U., Sap, J., Beug, H. and Vennstrom, B. (1988). Characterization of the hormone-binding domain of the chicken c-erbA/thyroid hormone receptor protein. EMBO J. 7,155 -159.[Abstract]
Nagy, L., Kao, H. Y., Chakravarti, D., Lin, R. J., Hassig, C. A., Ayer, D. E., Schreiber, S. L. and Evans, R. M. (1997). Nuclear receptor repression mediated by a complex containing SMRT, mSin3A, and histone deacetylase. Cell 89,373 -380.[Medline]
Nagy, L., Kao, H. Y., Love, J. D., Li, C., Banayo, E., Gooch, J.
T., Krishna, V., Chatterjee, K., Evans, R. M. and Schwabe, J. W.
(1999). Mechanism of co-repressor binding and release from
nuclear hormone receptors. Genes Dev.
13,3209
-3216.
Nakajima, H., Brindle, P. K., Handa, M. and Ihle, J. N.
(2001). Functional interaction of STAT5 and nuclear receptor
co-repressor SMRT: implications in negative regulation of STAT5-dependent
transcription. EMBO J.
20,6836
-6844.
Nan, X., Ng, H. H., Johnson, C. A., Laherty, C. D., Turner, B. M., Eisenman, R. N. and Bird, A. (1998). Transcriptional repression by the methyl-CpG-binding protein MeCP2 involves a histone deacetylase complex. Nature 393,386 -389.[Medline]
Nasmyth, K. A. (1982). The regulation of yeast mating-type chromatin structure by SIR: an action at a distance affecting both transcription and transposition. Cell 30,567 -578.[Medline]
Nasmyth, K., Stillman, D. and Kipling, D. (1987). Both positive and negative regulators of HO transcription are required for mother-cell-specific mating-type switching in yeast. Cell 48,579 -587.[Medline]
Nibu, Y., Zhang, H. and Levine, M. (1998).
Interaction of short-range repressors with Drosophila CtBP in the embryo.
Science 280,101
-104.
Nomura, T., Khan, M. M., Kaul, S. C., Dong, H. D., Wadhwa, R.,
Colmenares, C., Kohno, I. and Ishii, S. (1999). Ski is a
component of the histone deacetylase complex required for transcriptional
repression by Mad and thyroid hormone receptor. Genes
Dev. 13,412
-423.
Ordentlich, P., Downes, M., Xie, W., Genin, A., Spinner, N. B.
and Evans, R. M. (1999). Unique forms of human and mouse
nuclear receptor corepressor SMRT. Proc. Natl. Acad. Sci.
USA 96,2639
-2644.
Park, E. J., Schroen, D. J., Yang, M., Li, H., Li, L. and Chen,
J. D. (1999). SMRTe, a silencing mediator for retinoid and
thyroid hormone receptors-extended isoform that is more related to the nuclear
receptor co-repressor. Proc. Natl. Acad. Sci. USA
96,3519
-3524.
Paroush, Z., Finley, R. L., Jr, Kidd, T., Wainwright, S. M., Ingham, P. W., Brent, R. and Ish-Horowicz, D. (1994). Groucho is required for Drosophila neurogenesis, segmentation, and sex determination and interacts directly with hairy-related bHLH proteins. Cell 79,805 -815.[Medline]
Perissi, V., Staszewski, L. M., McInerney, E. M., Kurokawa, R.,
Krones, A., Rose, D. W., Lambert, M. H., Milburn, M. V., Glass, C. K. and
Rosenfeld, M. G. (1999). Molecular determinants of nuclear
receptor-co-repressor interaction. Genes Dev.
13,3198
-3208.
Poortinga, G., Watanabe, M. and Parkhurst, S. M.
(1998). Drosophila CtBP: a Hairy-interacting protein required for
embryonic segmentation and hairy-mediated transcriptional repression.
EMBO J. 17,2067
-2078.
Rine, J., Strathern, J. N., Hicks, J. B. and Herskowitz, I.
(1979). A suppressor of mating-type locus mutations in
Saccharomyces cerevisiae: evidence for and identification of cryptic
mating-type loci. Genetics
93,877
-901.
Rundlett, S. E., Carmen, A. A., Kobayashi, R., Bavykin, S.,
Turner, B. M. and Grunstein, M. (1996). HDA1 and RPD3 are
members of distinct yeast histone deacetylase complexes that regulate
silencing and transcription. Proc. Natl. Acad. Sci.
USA 93,14503
-14508.
Safer, J. D., Cohen, R. N., Hollenberg, A. N. and Wondisford, F.
E. (1998). Defective release of co-repressor by hinge mutants
of the thyroid hormone receptor found in patients with resistance to thyroid
hormone. J. Biol. Chem.
273,30175
-30182.
Sap, J., Munoz, A., Damm, K., Goldberg, Y., Ghysdael, J., Leutz, A., Beug, H. and Vennstrom, B. (1986). The c-erb-A protein is a high-affinity receptor for thyroid hormone. Nature 324,635 -640.[Medline]
Schaeper, U., Subramanian, T., Lim, L., Boyd, J. M. and
Chinnadurai, G. (1998). Interaction between a cellular
protein that binds to the C-terminal region of adenovirus E1A (CtBP) and a
novel cellular protein is disrupted by E1A through a conserved PLDLS motif.
J. Biol. Chem. 273,8549
-8552.
Seol, W., Mahon, M. J., Lee, Y. K. and Moore, D. D. (1996). Two receptor interacting domains in the nuclear hormone receptor co-repressor RIP13/N-CoR. Mol. Endocrinol. 10,1646 -1655.[Abstract]
Shang, Y., Hu, X., DiRenzo, J., Lazar, M. A. and Brown, M. (2000). Cofactor dynamics and sufficiency in estrogen receptor-regulated transcription. Cell 103,843 -852.[Medline]
Shanmugam, K., Green, N. C., Rambaldi, I., Saragovi, H. U. and
Featherstone, M. S. (1999). PBX and MEIS as non-DNA-binding
partners in trimeric complexes with HOX proteins. Mol. Cell.
Biol. 19,7577
-7588.
Shi, Y., Downes, M., Xie, W., Kao, H. Y., Ordentlich, P., Tsai,
C. C., Hon, M. and Evans, R. M. (2001). Sharp, an inducible
cofactor that integrates nuclear receptor repression and activation.
Genes Dev. 15,1140
-1151.
Shibata, H., Nawaz, Z., Tsai, S. Y., O'Malley, B. W. and Tsai,
M. J. (1997). Gene silencing by chicken ovalbumin upstream
promoter-transcription factor I (COUP-TFI) is mediated by transcriptional
co-repressors, nuclear receptor-co-repressor (N-CoR) and silencing mediator
for retinoic acid receptor and thyroid hormone receptor (SMRT).
Mol. Endocrinol. 11,714
-724.
Smith, C. L., Nawaz, Z. and O'Malley, B. W.
(1997). Coactivator and co-repressor regulation of the
agonist/antagonist activity of the mixed antiestrogen, 4-hydroxytamoxifen.
Mol. Endocrinol. 11,657
-666.
Smith, J. S., Brachmann, C. B., Celic, I., Kenna, M. A.,
Muhammad, S., Starai, V. J., Avalos, J. L., Escalante-Semerena, J. C.,
Grubmeyer, C., Wolberger, C. et al. (2000). A
phylogenetically conserved NAD+-dependent protein deacetylase activity in the
Sir2 protein family. Proc. Natl. Acad. Sci. USA
97,6658
-6663.
Steffan, J. S., Bodai, L., Pallos, J., Poelman, M., McCampbell, A., Apostol, B. L., Kazantsev, A., Schmidt, E., Zhu, Y. Z., Greenwald, M. et al. (2001). Histone deacetylase inhibitors arrest polyglutamine-dependent neurodegeneration in Drosophila. Nature 413,739 -743.[Medline]
Stroschein, S. L., Wang, W., Zhou, S., Zhou, Q. and Luo, K.
(1999). Negative feedback regulation of TGF-beta signaling by the
SnoN oncoprotein. Science
286,771
-774.
Tang, A. H., Neufeld, T. P., Kwan, E. and Rubin, G. M. (1997). PHYL acts to down-regulate TTK88, a transcriptional repressor of neuronal cell fates, by a SINA-dependent mechanism. Cell 90,459 -467.[Medline]
Tong, J. K., Hassig, C. A., Schnitzler, G. R., Kingston, R. E. and Schreiber, S. L. (1998). Chromatin deacetylation by an ATP-dependent nucleosome remodelling complex. Nature 395,917 -921.[Medline]
Tsang, A. W. and Escalante-Semerena, J. C.
(1998). CobB, a new member of the SIR2 family of eucaryotic
regulatory proteins, is required to compensate for the lack of nicotinate
mononucleotide: 5,6-dimethylbenzimidazole phosphoribosyltransferase activity
in cobT mutants during cobalamin biosynthesis in Salmonella
typhimurium LT2. J. Biol. Chem.
273,31788
-31794.
Turner, B. M. (1993). Decoding the nucleosome. Cell 75,5 -8.[Medline]
Turner, J. and Crossley, M. (2001). The CtBP family: enigmatic and enzymatic transcriptional co-repressors. BioEssays 23,683 -690.[Medline]
Underhill, C., Qutob, M. S., Yee, S. P. and Torchia, J.
(2000). A novel nuclear receptor co-repressor complex, N-CoR,
contains components of the mammalian SWI/SNF complex and the co-repressor
KAP-1. J. Biol. Chem.
275,40463
-40470.
Van Lint, C., Emiliani, S. and Verdin, E. (1996). The expression of a small fraction of cellular genes is changed in response to histone hyperacetylation. Gene Expr. 5,245 -253.[Medline]
Vannier, D., Balderes, D. and Shore, D. (1996).
Evidence that the transcriptional regulators SIN3 and RPD3, and a novel gene
(SDS3) with similar functions, are involved in transcriptional silencing in
S. cerevisiae. Genetics
144,1343
-1353.
Vaziri, H., Dessain, S. K., Eaton, E. N., Imai, S. I., Frye, R. A., Pandita, T. K., Guarente, L. and Weinberg, R. A. (2001). hSIR2SIRT1 Functions as an NAD-Dependent p53 Deacetylase. Cell 107,149 -160.[Medline]
Vidal, M. and Gaber, R. F. (1991). RPD3 encodes a second factor required to achieve maximum positive and negative transcriptional states in Saccharomyces cerevisiae. Mol. Cell. Biol. 11,6317 -6327.[Medline]
Vidal, M., Strich, R., Esposito, R. E. and Gaber, R. F. (1991). RPD1 (SIN3/UME4) is required for maximal activation and repression of diverse yeast genes. Mol. Cell. Biol. 11,6306 -6316.[Medline]
Wang, L. and Hiebert, S. W. (2001). TEL contacts multiple co-repressors and specifically associates with histone deacetylase-3. Oncogene 20,3716 -3725.[Medline]
Wang, J., Hoshino, T., Redner, R. L., Kajigaya, S. and Liu, J.
M. (1998). ETO, fusion partner in t(8;21) acute myeloid
leukemia, represses transcription by interaction with the human
N-CoR/mSin3/HDAC1 complex. Proc. Natl. Acad. Sci. USA
95,10860
-10865.
Wang, J., Saunthararajah, Y., Redner, R. L. and Liu, J. M.
(1999). Inhibitors of histone deacetylase relieve ETO-mediated
repression and induce differentiation of AML1-ETO leukemia cells.
Cancer Res. 59,2766
-2769.
Wen, Y. D., Perissi, V., Staszewski, L. M., Yang, W. M., Krones,
A., Glass, C. K., Rosenfeld, M. G. and Seto, E. (2000). The
histone deacetylase-3 complex contains nuclear receptor co-repressors.
Proc. Natl. Acad. Sci. USA
97,7202
-7207.
Winston, F. and Carlson, M. (1992). Yeast SNF/SWI transcriptional activators and the SPT/SIN chromatin connection. Trends Genet. 8,387 -391.[Medline]
Wong, C. W. and Privalsky, M. L. (1998).
Components of the SMRT co-repressor complex exhibit distinctive interactions
with the POZ domain oncoproteins PLZF, PLZF-RARalpha, and BCL-6. J.
Biol. Chem. 273,27695
-27702.
Wu, X., Li, H., Park, E. J. and Chen, J. D.
(2001). SMRTE inhibits MEF2C transcriptional activation by
targeting HDAC4 and 5 to nuclear domains. J. Biol.
Chem. 276,24177
-24185.
Xu, J., Nawaz, Z., Tsai, S. Y., Tsai, M. J. and O'Malley, B.
W. (1996). The extreme C terminus of progesterone receptor
contains a transcriptional repressor domain that functions through a putative
co-repressor. Proc. Natl. Acad. Sci. USA
93,12195
-12199.
Xu, L., Lavinsky, R. M., Dasen, J. S., Flynn, S. E., McInerney, E. M., Mullen, T. M., Heinzel, T., Szeto, D., Korzus, E., Kurokawa, R. et al. (1998). Signal-specific co-activator domain requirements for Pit-1 activation. Nature 395,301 -306.[Medline]
Xue, Y., Wong, J., Moreno, G. T., Young, M. K., Cote, J. and Wang, W. (1998). NURD, a novel complex with both ATP-dependent chromatin-remodeling and histone deacetylase activities. Mol. Cell 2,851 -861.[Medline]
Yoh, S. M., Chatterjee, V. K. and Privalsky, M. L.
(1997). Thyroid hormone resistance syndrome manifests as an
aberrant interaction between mutant T3 receptors and transcriptional
co-repressors. Mol. Endocrinol.
11,470
-480.
You, A., Tong, J. K., Grozinger, C. M. and Schreiber, S. L.
(2001). CoREST is an integral component of the CoREST- human
histone deacetylase complex. Proc Natl Acad Sci USA
98,1454
-1458.
Zamir, I., Harding, H. P., Atkins, G. B., Horlein, A., Glass, C. K., Rosenfeld, M. G. and Lazar, M. A. (1996). A nuclear hormone receptor co-repressor mediates transcriptional silencing by receptors with distinct repression domains. Mol. Cell. Biol. 16,5458 -5465.[Abstract]
Zhang, Y., Iratni, R., Erdjument-Bromage, H., Tempst, P. and Reinberg, D. (1997). Histone deacetylases and SAP18, a novel polypeptide, are components of a human Sin3 complex. Cell 89,357 -364.[Medline]
Zhang, J., Guenther, M. G., Carthew, R. W. and Lazar, M. A.
(1998a). Proteasomal regulation of nuclear receptor
co-repressor-mediated repression. Genes Dev.
12,1775
-1780.
Zhang, Y., LeRoy, G., Seelig, H. P., Lane, W. S. and Reinberg, D. (1998b). The dermatomyositis-specific autoantigen Mi2 is a component of a complex containing histone deacetylase and nucleosome remodeling activities. Cell 95,279 -289.[Medline]
Zhang, Y., Sun, Z. W., Iratni, R., Erdjument-Bromage, H., Tempst, P., Hampsey, M. and Reinberg, D. (1998c). SAP30, a novel protein conserved between human and yeast, is a component of a histone deacetylase complex. Mol. Cell 1,1021 -1031.[Medline]
Zhang, Y., Ng, H. H., Erdjument-Bromage, H., Tempst, P., Bird,
A. and Reinberg, D. (1999). Analysis of the NuRD subunits
reveals a histone deacetylase core complex and a connection with DNA
methylation. Genes Dev.
13,1924
-1935.
Zhou, S. and Hayward, S. D. (2001). Nuclear
localization of cbf1 is regulated by interactions with the smrt co-repressor
complex. Mol. Cell. Biol.
21,6222
-6232.
Zhou, Y., Gross, W., Hong, S. H. and Privalsky, M. L. (2001). The SMRT co-repressor is a target of phosphorylation by protein kinase CK2 (casein kinase II). Mol. Cell. Biochem. 220,1 -13.[Medline]
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