Ignet

Gene Information

Gene symbol: HDAC3

Gene name: histone deacetylase 3

HGNC ID: 4854

Synonyms: RPD3, HD3, RPD3-2

Related Genes

#	Gene Symbol	Number of hits
1	AKAP8	1 hits
2	AKAP8L	1 hits
3	ARNTL	1 hits
4	AURKB	1 hits
5	ESRRB	1 hits
6	HDAC1	1 hits
7	HDAC4	1 hits
8	HDAC9	1 hits
9	HIST4H4	1 hits
10	IL4	1 hits
11	MARVELD2	1 hits
12	NCOR1	1 hits
13	NCOR2	1 hits
14	SMARCA5	1 hits
15	TBL1X	1 hits
16	XRCC6	1 hits

Related Sentences

#	PMID	Sentence
1	10809664	A core SMRT corepressor complex containing HDAC3 and TBL1, a WD40-repeat protein linked to deafness.
2	10809664	It also contains HDAC3, a histone deacetylase not previously thought to interact with SMRT.
3	10809664	TBL1 displays structural and functional similarities to Tup1 and Groucho corepressors, sharing their ability to interact with histone H3.
4	10809664	In vivo, TBL1 is bridged to HDAC3 through SMRT and can potentiate repression by TR.
5	10809664	A core SMRT corepressor complex containing HDAC3 and TBL1, a WD40-repeat protein linked to deafness.
6	10809664	It also contains HDAC3, a histone deacetylase not previously thought to interact with SMRT.
7	10809664	TBL1 displays structural and functional similarities to Tup1 and Groucho corepressors, sharing their ability to interact with histone H3.
8	10809664	In vivo, TBL1 is bridged to HDAC3 through SMRT and can potentiate repression by TR.
9	10809664	A core SMRT corepressor complex containing HDAC3 and TBL1, a WD40-repeat protein linked to deafness.
10	10809664	It also contains HDAC3, a histone deacetylase not previously thought to interact with SMRT.
11	10809664	TBL1 displays structural and functional similarities to Tup1 and Groucho corepressors, sharing their ability to interact with histone H3.
12	10809664	In vivo, TBL1 is bridged to HDAC3 through SMRT and can potentiate repression by TR.
13	11509652	The SMRT and N-CoR corepressors are activating cofactors for histone deacetylase 3.
14	11509652	A cognate DAD is present in the related corepressor N-CoR, which can also activate HDAC3.
15	11509652	Mutations in the DAD that abolish HDAC3 interaction also eliminate reconstitution of HDAC activity.
16	11509652	Thus, SMRT and N-CoR do not serve merely as platforms for HDAC recruitment but function as an integral component of an active cellular HDAC3 enzyme.
17	11509652	The SMRT and N-CoR corepressors are activating cofactors for histone deacetylase 3.
18	11509652	A cognate DAD is present in the related corepressor N-CoR, which can also activate HDAC3.
19	11509652	Mutations in the DAD that abolish HDAC3 interaction also eliminate reconstitution of HDAC activity.
20	11509652	Thus, SMRT and N-CoR do not serve merely as platforms for HDAC recruitment but function as an integral component of an active cellular HDAC3 enzyme.
21	11509652	The SMRT and N-CoR corepressors are activating cofactors for histone deacetylase 3.
22	11509652	A cognate DAD is present in the related corepressor N-CoR, which can also activate HDAC3.
23	11509652	Mutations in the DAD that abolish HDAC3 interaction also eliminate reconstitution of HDAC activity.
24	11509652	Thus, SMRT and N-CoR do not serve merely as platforms for HDAC recruitment but function as an integral component of an active cellular HDAC3 enzyme.
25	11509652	The SMRT and N-CoR corepressors are activating cofactors for histone deacetylase 3.
26	11509652	A cognate DAD is present in the related corepressor N-CoR, which can also activate HDAC3.
27	11509652	Mutations in the DAD that abolish HDAC3 interaction also eliminate reconstitution of HDAC activity.
28	11509652	Thus, SMRT and N-CoR do not serve merely as platforms for HDAC recruitment but function as an integral component of an active cellular HDAC3 enzyme.
29	12502735	Assembly of the SMRT-histone deacetylase 3 repression complex requires the TCP-1 ring complex.
30	12502735	Histone deacetylase 3 (HDAC3) requires the nuclear receptor corepressor SMRT for HDAC enzyme activity.
31	12502735	Here we report that HDAC3 interacts with SMRT only after priming by cellular chaperones including the TCP-1 ring complex (TRiC), which is required for proper folding of HDAC3 in an ATP-dependent process.
32	12502735	SMRT displaces TRiC from HDAC3, yielding an active HDAC enzyme.
33	12502735	Assembly of the SMRT-histone deacetylase 3 repression complex requires the TCP-1 ring complex.
34	12502735	Histone deacetylase 3 (HDAC3) requires the nuclear receptor corepressor SMRT for HDAC enzyme activity.
35	12502735	Here we report that HDAC3 interacts with SMRT only after priming by cellular chaperones including the TCP-1 ring complex (TRiC), which is required for proper folding of HDAC3 in an ATP-dependent process.
36	12502735	SMRT displaces TRiC from HDAC3, yielding an active HDAC enzyme.
37	12502735	Assembly of the SMRT-histone deacetylase 3 repression complex requires the TCP-1 ring complex.
38	12502735	Histone deacetylase 3 (HDAC3) requires the nuclear receptor corepressor SMRT for HDAC enzyme activity.
39	12502735	Here we report that HDAC3 interacts with SMRT only after priming by cellular chaperones including the TCP-1 ring complex (TRiC), which is required for proper folding of HDAC3 in an ATP-dependent process.
40	12502735	SMRT displaces TRiC from HDAC3, yielding an active HDAC enzyme.
41	12502735	Assembly of the SMRT-histone deacetylase 3 repression complex requires the TCP-1 ring complex.
42	12502735	Histone deacetylase 3 (HDAC3) requires the nuclear receptor corepressor SMRT for HDAC enzyme activity.
43	12502735	Here we report that HDAC3 interacts with SMRT only after priming by cellular chaperones including the TCP-1 ring complex (TRiC), which is required for proper folding of HDAC3 in an ATP-dependent process.
44	12502735	SMRT displaces TRiC from HDAC3, yielding an active HDAC enzyme.
45	12861000	The N-CoR/histone deacetylase 3 complex is required for repression by thyroid hormone receptor.
46	12861000	Nuclear receptor corepressors (N-CoR) and silencing mediator for retinoid and thyroid receptors (SMRT) have both been implicated in thyroid hormone receptor (TR)-mediated repression.
47	12861000	Here we show that endogenous N-CoR, TBL1, and histone deacetylase 3 (HDAC3), but not HDAC1, -2, or -4, are recruited to a stably integrated reporter gene repressed by unliganded TR as well as the orphan receptor RevErb.
48	12861000	Knockdown of N-CoR using small interfering RNAs markedly reduces repression by the TR ligand binding domain in human 293T cells, whereas knockdown of SMRT has little effect.
49	12861000	Knockdown of HDAC3 markedly reduces repression by both TR and RevErb, while knockdown of HDAC1 or 2 has more modest, partly nonspecific effects.
50	12861000	Thus, HDAC3 is critical for repression by multiple nuclear receptors and the N-CoR HDAC3 complex plays a unique and necessary role in TR-mediated gene repression in human 293T cells.
51	12861000	The N-CoR/histone deacetylase 3 complex is required for repression by thyroid hormone receptor.
52	12861000	Nuclear receptor corepressors (N-CoR) and silencing mediator for retinoid and thyroid receptors (SMRT) have both been implicated in thyroid hormone receptor (TR)-mediated repression.
53	12861000	Here we show that endogenous N-CoR, TBL1, and histone deacetylase 3 (HDAC3), but not HDAC1, -2, or -4, are recruited to a stably integrated reporter gene repressed by unliganded TR as well as the orphan receptor RevErb.
54	12861000	Knockdown of N-CoR using small interfering RNAs markedly reduces repression by the TR ligand binding domain in human 293T cells, whereas knockdown of SMRT has little effect.
55	12861000	Knockdown of HDAC3 markedly reduces repression by both TR and RevErb, while knockdown of HDAC1 or 2 has more modest, partly nonspecific effects.
56	12861000	Thus, HDAC3 is critical for repression by multiple nuclear receptors and the N-CoR HDAC3 complex plays a unique and necessary role in TR-mediated gene repression in human 293T cells.
57	12861000	The N-CoR/histone deacetylase 3 complex is required for repression by thyroid hormone receptor.
58	12861000	Nuclear receptor corepressors (N-CoR) and silencing mediator for retinoid and thyroid receptors (SMRT) have both been implicated in thyroid hormone receptor (TR)-mediated repression.
59	12861000	Here we show that endogenous N-CoR, TBL1, and histone deacetylase 3 (HDAC3), but not HDAC1, -2, or -4, are recruited to a stably integrated reporter gene repressed by unliganded TR as well as the orphan receptor RevErb.
60	12861000	Knockdown of N-CoR using small interfering RNAs markedly reduces repression by the TR ligand binding domain in human 293T cells, whereas knockdown of SMRT has little effect.
61	12861000	Knockdown of HDAC3 markedly reduces repression by both TR and RevErb, while knockdown of HDAC1 or 2 has more modest, partly nonspecific effects.
62	12861000	Thus, HDAC3 is critical for repression by multiple nuclear receptors and the N-CoR HDAC3 complex plays a unique and necessary role in TR-mediated gene repression in human 293T cells.
63	12861000	The N-CoR/histone deacetylase 3 complex is required for repression by thyroid hormone receptor.
64	12861000	Nuclear receptor corepressors (N-CoR) and silencing mediator for retinoid and thyroid receptors (SMRT) have both been implicated in thyroid hormone receptor (TR)-mediated repression.
65	12861000	Here we show that endogenous N-CoR, TBL1, and histone deacetylase 3 (HDAC3), but not HDAC1, -2, or -4, are recruited to a stably integrated reporter gene repressed by unliganded TR as well as the orphan receptor RevErb.
66	12861000	Knockdown of N-CoR using small interfering RNAs markedly reduces repression by the TR ligand binding domain in human 293T cells, whereas knockdown of SMRT has little effect.
67	12861000	Knockdown of HDAC3 markedly reduces repression by both TR and RevErb, while knockdown of HDAC1 or 2 has more modest, partly nonspecific effects.
68	12861000	Thus, HDAC3 is critical for repression by multiple nuclear receptors and the N-CoR HDAC3 complex plays a unique and necessary role in TR-mediated gene repression in human 293T cells.
69	15695367	Although the N-terminal RD binds transducin beta-like protein 1 (TBL1), TBLR1, and mSin3, deletion of this region did not affect the ability of N-CoR to mediate repression by TR.
70	15695367	By contrast, deletion of the deacetylase activating domain (DAD) that binds and activates histone deacetylase 3 dramatically hampered N-CoR's function as a TR corepressor.
71	15761026	The orphan nuclear receptor Rev-erbalpha recruits the N-CoR/histone deacetylase 3 corepressor to regulate the circadian Bmal1 gene.
72	15761026	Rev-erbalpha directly binds to the mouse Bmal1 promoter and recruits the endogenous nuclear receptor corepressor (N-CoR)/histone deacetylase 3 (HDAC3) complex, in association with a decrease in histone acetylation.
73	15761026	The endogenous N-CoR/HDAC3 complex is also associated with the endogenous Bmal1 promoter in human HepG2 liver cells, where a reduction in cellular HDAC3 level markedly increases the expression of Bmal1 mRNA.
74	15761026	These data demonstrate a new function for the N-CoR/HDAC3 complex in regulating the expression of genes involved in circadian rhythm by functioning as corepressor for Rev-erbalpha.
75	15761026	The orphan nuclear receptor Rev-erbalpha recruits the N-CoR/histone deacetylase 3 corepressor to regulate the circadian Bmal1 gene.
76	15761026	Rev-erbalpha directly binds to the mouse Bmal1 promoter and recruits the endogenous nuclear receptor corepressor (N-CoR)/histone deacetylase 3 (HDAC3) complex, in association with a decrease in histone acetylation.
77	15761026	The endogenous N-CoR/HDAC3 complex is also associated with the endogenous Bmal1 promoter in human HepG2 liver cells, where a reduction in cellular HDAC3 level markedly increases the expression of Bmal1 mRNA.
78	15761026	These data demonstrate a new function for the N-CoR/HDAC3 complex in regulating the expression of genes involved in circadian rhythm by functioning as corepressor for Rev-erbalpha.
79	15761026	The orphan nuclear receptor Rev-erbalpha recruits the N-CoR/histone deacetylase 3 corepressor to regulate the circadian Bmal1 gene.
80	15761026	Rev-erbalpha directly binds to the mouse Bmal1 promoter and recruits the endogenous nuclear receptor corepressor (N-CoR)/histone deacetylase 3 (HDAC3) complex, in association with a decrease in histone acetylation.
81	15761026	The endogenous N-CoR/HDAC3 complex is also associated with the endogenous Bmal1 promoter in human HepG2 liver cells, where a reduction in cellular HDAC3 level markedly increases the expression of Bmal1 mRNA.
82	15761026	These data demonstrate a new function for the N-CoR/HDAC3 complex in regulating the expression of genes involved in circadian rhythm by functioning as corepressor for Rev-erbalpha.
83	15761026	The orphan nuclear receptor Rev-erbalpha recruits the N-CoR/histone deacetylase 3 corepressor to regulate the circadian Bmal1 gene.
84	15761026	Rev-erbalpha directly binds to the mouse Bmal1 promoter and recruits the endogenous nuclear receptor corepressor (N-CoR)/histone deacetylase 3 (HDAC3) complex, in association with a decrease in histone acetylation.
85	15761026	The endogenous N-CoR/HDAC3 complex is also associated with the endogenous Bmal1 promoter in human HepG2 liver cells, where a reduction in cellular HDAC3 level markedly increases the expression of Bmal1 mRNA.
86	15761026	These data demonstrate a new function for the N-CoR/HDAC3 complex in regulating the expression of genes involved in circadian rhythm by functioning as corepressor for Rev-erbalpha.
87	15832170	As expected, repression is characterized by recruitment of N-CoR/SMRT-HDAC3 (histone deacetylase 3) co-repressor complexes, leading to local histone hypoacetylation.
88	15832170	This order is determined by the inherent substrate specificity of HDAC3, and unexpectedly predicts the binding preference of N-CoR/SMRT for submaximally acetylated H4 tails.
89	15832170	The match between the specificity of acetyl-histone deacetylation by HDAC3 and the histone-binding preference of N-CoR/SMRT allows the co-repressor complex to stabilize and propagate repression of nuclear hormone receptor gene targets.
90	15832170	As expected, repression is characterized by recruitment of N-CoR/SMRT-HDAC3 (histone deacetylase 3) co-repressor complexes, leading to local histone hypoacetylation.
91	15832170	This order is determined by the inherent substrate specificity of HDAC3, and unexpectedly predicts the binding preference of N-CoR/SMRT for submaximally acetylated H4 tails.
92	15832170	The match between the specificity of acetyl-histone deacetylation by HDAC3 and the histone-binding preference of N-CoR/SMRT allows the co-repressor complex to stabilize and propagate repression of nuclear hormone receptor gene targets.
93	15832170	As expected, repression is characterized by recruitment of N-CoR/SMRT-HDAC3 (histone deacetylase 3) co-repressor complexes, leading to local histone hypoacetylation.
94	15832170	This order is determined by the inherent substrate specificity of HDAC3, and unexpectedly predicts the binding preference of N-CoR/SMRT for submaximally acetylated H4 tails.
95	15832170	The match between the specificity of acetyl-histone deacetylation by HDAC3 and the histone-binding preference of N-CoR/SMRT allows the co-repressor complex to stabilize and propagate repression of nuclear hormone receptor gene targets.
96	16917504	The N-CoR complex enables chromatin remodeler SNF2H to enhance repression by thyroid hormone receptor.
97	16917504	Unliganded thyroid hormone receptor (TR) actively represses transcription via the nuclear receptor corepressor (N-CoR)/histone deacetylase 3 (HDAC3) complex.
98	16917504	N-CoR and HDAC3 are both required for recruitment of SNF2H to the repressed gene.
99	16917504	SNF2H does not interact directly with the N-CoR/HDAC3 complex, but binds to unacetylated histone H4 tails, suggesting that deacetylase activity of the corepressor complex is critical to SNF2H function.
100	16917504	Indeed, HDAC3 as well as SNF2H are required for nucleosomal organization on the TR target gene.
101	16917504	Consistent with these findings, reduction of SNF2H induces expression of an endogenous TR-regulated gene, dio1, in liver cells.
102	16917504	The N-CoR complex enables chromatin remodeler SNF2H to enhance repression by thyroid hormone receptor.
103	16917504	Unliganded thyroid hormone receptor (TR) actively represses transcription via the nuclear receptor corepressor (N-CoR)/histone deacetylase 3 (HDAC3) complex.
104	16917504	N-CoR and HDAC3 are both required for recruitment of SNF2H to the repressed gene.
105	16917504	SNF2H does not interact directly with the N-CoR/HDAC3 complex, but binds to unacetylated histone H4 tails, suggesting that deacetylase activity of the corepressor complex is critical to SNF2H function.
106	16917504	Indeed, HDAC3 as well as SNF2H are required for nucleosomal organization on the TR target gene.
107	16917504	Consistent with these findings, reduction of SNF2H induces expression of an endogenous TR-regulated gene, dio1, in liver cells.
108	16917504	The N-CoR complex enables chromatin remodeler SNF2H to enhance repression by thyroid hormone receptor.
109	16917504	Unliganded thyroid hormone receptor (TR) actively represses transcription via the nuclear receptor corepressor (N-CoR)/histone deacetylase 3 (HDAC3) complex.
110	16917504	N-CoR and HDAC3 are both required for recruitment of SNF2H to the repressed gene.
111	16917504	SNF2H does not interact directly with the N-CoR/HDAC3 complex, but binds to unacetylated histone H4 tails, suggesting that deacetylase activity of the corepressor complex is critical to SNF2H function.
112	16917504	Indeed, HDAC3 as well as SNF2H are required for nucleosomal organization on the TR target gene.
113	16917504	Consistent with these findings, reduction of SNF2H induces expression of an endogenous TR-regulated gene, dio1, in liver cells.
114	16917504	The N-CoR complex enables chromatin remodeler SNF2H to enhance repression by thyroid hormone receptor.
115	16917504	Unliganded thyroid hormone receptor (TR) actively represses transcription via the nuclear receptor corepressor (N-CoR)/histone deacetylase 3 (HDAC3) complex.
116	16917504	N-CoR and HDAC3 are both required for recruitment of SNF2H to the repressed gene.
117	16917504	SNF2H does not interact directly with the N-CoR/HDAC3 complex, but binds to unacetylated histone H4 tails, suggesting that deacetylase activity of the corepressor complex is critical to SNF2H function.
118	16917504	Indeed, HDAC3 as well as SNF2H are required for nucleosomal organization on the TR target gene.
119	16917504	Consistent with these findings, reduction of SNF2H induces expression of an endogenous TR-regulated gene, dio1, in liver cells.
120	16980585	HDAC3 forms a complex with A-Kinase-Anchoring Proteins AKAP95 and HA95, which are targeted to mitotic chromosomes.
121	16980585	Deacetylation of H3 in mitosis requires AKAP95/HA95 and HDAC3 and provides a hypoacetylated H3 tail that is the preferred substrate for Aurora B kinase.
122	16980585	Phosphorylation of H3S10 by Aurora B leads to dissociation of HP1 proteins from methylated H3K9 residues on mitotic heterochromatin.
123	16980585	HDAC3 forms a complex with A-Kinase-Anchoring Proteins AKAP95 and HA95, which are targeted to mitotic chromosomes.
124	16980585	Deacetylation of H3 in mitosis requires AKAP95/HA95 and HDAC3 and provides a hypoacetylated H3 tail that is the preferred substrate for Aurora B kinase.
125	16980585	Phosphorylation of H3S10 by Aurora B leads to dissociation of HP1 proteins from methylated H3K9 residues on mitotic heterochromatin.
126	16982777	We unexpectedly found that the corepressor silencing mediator for retinoid and thyroid hormone receptor (SMRT) associates with the DNA-PK repair complex.
127	16982777	The SMRT/histone deacetylase 3 complex is required for the transcriptional repressive property of the Ku70 subunit of the repair complex.
128	19710360	Heme binding to Rev-erbalpha recruits the NCoR/histone deacetylase 3 (HDAC3) corepressor complex to repress the transcription of the coactivator PGC-1alpha, a potent inducer of heme synthesis.
129	20427468	In the absence of TH, TH receptors repress genes that are TH-activated by recruiting the nuclear receptor corepressor (NCoR), which exists in a tight complex with histone deacetylase 3 (HDAC3).
130	20427468	Thus, the NCoR interaction with HDAC3 modulates expression of both positively- and negatively-regulated genes by TH in vivo.
131	20427468	In the absence of TH, TH receptors repress genes that are TH-activated by recruiting the nuclear receptor corepressor (NCoR), which exists in a tight complex with histone deacetylase 3 (HDAC3).
132	20427468	Thus, the NCoR interaction with HDAC3 modulates expression of both positively- and negatively-regulated genes by TH in vivo.
133	21565617	We show here that in liver, class IIa HDACs (HDAC4, 5, and 7) are phosphorylated and excluded from the nucleus by AMPK family kinases.
134	21565617	In turn, HDAC4/5 recruit HDAC3, which results in the acute transcriptional induction of these genes via deacetylation and activation of FOXO family transcription factors.
135	22156208	Here we report that macrophages lacking histone deacetylase 3 (HDAC3) display a polarization phenotype similar to IL-4-induced alternative activation and, furthermore, are hyperresponsive to IL-4 stimulation.
136	22156208	Throughout the macrophage genome, HDAC3 deacetylates histone tails at regulatory regions, leading to repression of many IL-4-regulated genes characteristic of alternative activation.
137	22156208	Here we report that macrophages lacking histone deacetylase 3 (HDAC3) display a polarization phenotype similar to IL-4-induced alternative activation and, furthermore, are hyperresponsive to IL-4 stimulation.
138	22156208	Throughout the macrophage genome, HDAC3 deacetylates histone tails at regulatory regions, leading to repression of many IL-4-regulated genes characteristic of alternative activation.
139	23292142	In vitro, HDAC3 protein itself has minimal enzyme activity but gains its histone-deacetylation function from stable association with the conserved deacetylase-activating domain (DAD) contained in nuclear receptor co-repressors NCOR1 and SMRT.
140	23292142	Here we show that HDAC3 enzyme activity is undetectable in mice bearing point mutations in the DAD of both NCOR1 and SMRT (NS-DADm), despite having normal levels of HDAC3 protein.
141	23292142	In vitro, HDAC3 protein itself has minimal enzyme activity but gains its histone-deacetylation function from stable association with the conserved deacetylase-activating domain (DAD) contained in nuclear receptor co-repressors NCOR1 and SMRT.
142	23292142	Here we show that HDAC3 enzyme activity is undetectable in mice bearing point mutations in the DAD of both NCOR1 and SMRT (NS-DADm), despite having normal levels of HDAC3 protein.