JDP2, a Repressor of AP-1, Recruits a Histone Deacetylase 3 Complex To Inhibit the Retinoic Acid-Induced Differentiation of F9 Cells

Jin, Chunyuan; Li, Hongjie; Murata, Takehide; Sun, Kun; Horikoshi, Masami; Chiu, Robert; Yokoyama, Kazunari K.

doi:10.1128/mcb.22.13.4815-4826.2002

Cited by 96 publications

(118 citation statements)

References 46 publications

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“…18 Moreover, we showed also that JDP2 can act directly to inhibit the histone acetyltransferase (HAT) activity induced by p300 in undifferentiated F9 cells and that it induces chromatin assembly. 24 In the presence of RA, JDP2 and HDAC3 were excluded from the differentiation response element (DRE) site and p300 HAT was recruited to this site during the RA-induced differentiation of F9 cells.…”

Section: Resultsmentioning

confidence: 90%

“…Since JDP2 promotes the spontaneous differentiation of C2C12 cells 16 and since ectopic JDP2 inhibits the RA-induced differentiation of F9 cells, 18 we examined the effects of endogenous JDP2 on the differentiation of MEFs to adipocytes. We exposed confluent MEFs to differentiation medium for 2, 3 or 4 days and then incubated them in growth medium that contained insulin (insulin-GM).…”

Section: Resultsmentioning

confidence: 99%

“…Co-immunoprecipitation (co-IP)assay and Western blotting revealed that JDP2 associated with HDAC3 in Cos-1 cells in vivo (Figure 6g), a result that was consistent with results reported previously in a different system. 18 Additional ChIP assays with antibodies against p300 demonstrated that p300, recruited to the promoter of the C/EBPd gene (Figure 6h), probably contributed to histone acetylation via its histone acetyltransferase (HAT) activity. The p300 protein recruited to the C/EBPd promoter was more ChIP assays with antibodies against (e) acetyl H3, (f) HDAC3 and (h) p300 and the same cell extracts as those in the experiment for which results are shown in (a).…”

Section: Resultsmentioning

confidence: 99%

“…12,13 Jun dimerization protein 2 (JDP2) is a DNA-binding protein that forms homodimers or heterodimers with c-Jun, ATF2 and C/EBPg. [14][15][16] JDP2 can function not only as a transcriptional repressor but also as a coactivator in various types of cell, 15,[17][18][19][20] and it is involved in a variety of biological phenomena such as proliferation and differentiation of cells and apoptosis. 14,15,17,18,[20][21][22] For example, forced expression of JDP2 represses the retinoic acid-mediated (RA-mediated) transcription of the c-jun gene and the differentiation of F9 cells in response to RA.…”

mentioning

confidence: 99%

“…14,15,17,18,[20][21][22] For example, forced expression of JDP2 represses the retinoic acid-mediated (RA-mediated) transcription of the c-jun gene and the differentiation of F9 cells in response to RA. 18 By contrast, the expression of an exogenous gene for JDP2 promotes the formation of C2 myotube and strong expression of major myogenic markers in C2 myoblasts. 16 Moreover, ectopic expression of JDP2 in rhabdomyosarcoma cells induces myogenesis and the formation of incomplete myotubes.…”

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confidence: 99%

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JDP2 suppresses adipocyte differentiation by regulating histone acetylation

Nakade¹,

Pan²,

Yoshiki

et al. 2007

Cell Death Differ

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Among the events that control cellular differentiation, the acetylation of histones plays a critical role in the regulation of transcription and the modification of chromatin. Jun dimerization protein 2 (JDP2), a member of the AP-1 family, is an inhibitor of such acetylation and contributes to the maintenance of chromatin structure. In an examination of Jdp2 'knock-out' (KO) mice, we observed elevated numbers of white adipocytes and significant accumulation of lipid in the adipose tissue in sections of scapulae. In addition, mouse embryo fibroblasts (MEFs) from Jdp2 KO mice were more susceptible to adipocyte differentiation in response to hormonal induction and members of the CCAAT/enhancer-binding proteins (C/EBP) gene family were expressed at levels higher than MEFs from wild-type mice. Furthermore, JDP2 inhibited both the acetylation of histone H3 in the promoter of the gene for C/EBPd and transcription from this promoter. Our data indicate that JDP2 plays a key role as a repressor of adipocyte differentiation by regulating the expression of the gene for C/EBPd via inhibition of histone acetylation.

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Section: Resultsmentioning

confidence: 90%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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JDP2 suppresses adipocyte differentiation by regulating histone acetylation

Nakade¹,

Pan²,

Yoshiki

et al. 2007

Cell Death Differ

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Amino acids as regulators of gene expression in mammals: Molecular mechanisms

Bruhat¹,

Chérasse²,

Chaveroux³

et al. 2009

BioFactors

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In mammals, the impact of nutrients on gene expression has become an important area of research. Because amino acids have multiple and important functions, their homeostasis has to be finely maintained. However, amino acidemia can be affected in some nutritional conditions and by various forms of stress. Consequently, mammals have to adjust physiological functions involved in the adaptation to amino acid availability. Part of this regulation involves the modulation of numerous gene expression. It has been shown that amino acids by themselves can modify the expression of target genes. This review focuses on the recent advances in the understanding of the mechanisms involved in the control of mammalian gene expression in response to amino acid limitation.

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Nanog regulates molecules involved in stemness and cell cycle‐signaling pathway for maintenance of pluripotency of P19 embryonal carcinoma stem cells

Choi

Park

et al. 2012

Journal Cellular Physiology

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To identify potential downstream targets of Nanog, a key transcription factor in the maintenance of pluripotency of embryonic stem (ES) and embryonal carcinoma (EC) cells, global gene expression profiles in Nanog small interfering RNA (siRNA)-transfected P19 EC stem cells were performed using cDNA, 60-mer, and 30-mer microarray platforms. The putative Nanog target genes identified by Nanog silencing were verified using reverse transcription-polymerase chain reaction after Nanog overexpression. Downregulation of Nanog in P19 cells resulted in reduction of pluripotency markers, such as Fgf4, Klf2, Mtf2, Oct-4, Rex1, Sox1, Yes, and Zfp143, whereas overexpression of Nanog in P19 cells reversely upregulated their expression. However, expressions of pluripotency markers Cripto, germ cell nuclear factor, Sox2, and Zfp57 as well as leukemia inhibitory factor (LIF)/Stat3 pathway molecules LIF, IL6st, and Stat3 were not affected after 48 h transfection with Nanog siRNA or construct. Nanog silencing also downregulated expression of molecules involved in the p53- and cell cycle-signaling pathway (Atf3, Jdp2, Cul3, Hist1hic, and Bcl6), whereas expression of E2f1, Tob1, Lyn, and Smarcc1 was upregulated by Nanog silencing. Expressions of cyclins D1, D2, D3, and E1 as well as cyclin-dependent kinase (Cdk) 1 and Cdk6 were downregulated by Nanog silencing in P19 cells, whereas Nanog overexpression reversely increased their expressions. Taken together, examination of global transcriptional changes after Nanog silencing followed by verification by Nanog overexpression has revealed new molecules involved in the maintenance of self-renewal and in the regulation of the p53- and cell cycle-pathway of P19 cells.

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JDP2, a Repressor of AP-1, Recruits a Histone Deacetylase 3 Complex To Inhibit the Retinoic Acid-Induced Differentiation of F9 Cells

Cited by 96 publications

References 46 publications

JDP2 suppresses adipocyte differentiation by regulating histone acetylation

JDP2 suppresses adipocyte differentiation by regulating histone acetylation

Amino acids as regulators of gene expression in mammals: Molecular mechanisms

Nanog regulates molecules involved in stemness and cell cycle‐signaling pathway for maintenance of pluripotency of P19 embryonal carcinoma stem cells

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