JDP2 suppresses adipocyte differentiation by regulating histone acetylation

Nakade, Koji; Pan, Jiaping; Yoshiki, Atsushi; Ugai, Hideyo; Kimura, Makoto; Liu, B; Li, H; Obata, Yuichi; Iwama, Mizuho; Itohara, Shigeyoshi; Murata, Takehide; Yokoyama, Kazunari K.

doi:10.1038/sj.cdd.4402129

Cited by 52 publications

(79 citation statements)

References 37 publications

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“…JDP2 has effects on various cellular processes. It mediates the differentiation of myoblasts [5] and osteoclasts [6], inhibits the differentiation of adipocytes [7] and embryonic carcinoma cells [8], acts as a tumor suppressor in NIH3T3 cells and prostate cancer cell lines [9], induces the partial transformation of chick embryonic fibroblasts [10], and functions as a cell-survival protein [11] and as a progesterone receptor coactivator [12]. The mechanisms of JDP2-mediated transcriptional repression may include the regulation of nucleosome assembly and histone acetylation [13].…”

Section: Introductionmentioning

confidence: 99%

IRF2‐binding protein‐1 is a JDP2 ubiquitin ligase and an inhibitor of ATF2‐dependent transcription

Kimura¹

2008

FEBS Letters

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Jun-dimerization protein 2 (JDP2) is a member of the activating protein-1 (AP-1) family of transcription factors. JDP2 dimerizes with other AP-1 proteins such as activating transcription factor-2 (ATF2) and Jun to repress transcription from promoters that contain a cyclic AMP-responsive element (CRE). Interferon regulatory factor-2-binding protein-1 (IRF2-BP1), which is reported to be a transcriptional corepressor of IRF2, was isolated as a JDP2-binding protein using an epitope-tagging method. As anticipated from the presence of a RING-finger domain, IRF2-BP1 enhanced the polyubiquitination of JDP2. Moreover, IRF2-BP1 repressed ATF2-mediated transcriptional activation from a CRE-containing promoter.

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Section: Introductionmentioning

confidence: 99%

IRF2‐binding protein‐1 is a JDP2 ubiquitin ligase and an inhibitor of ATF2‐dependent transcription

Kimura¹

2008

FEBS Letters

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“…Immortalized WT MEF were generated by serial passaging in 20% O 2 for 80 days. The generation of Jdp2 "knock-out" mice has been described elsewhere (34).…”

Section: Transgenic Mice and Mef-we Generated Jdp2mentioning

confidence: 99%

“…After 2 days, cells were stored frozen as "fresh MEF. " Genotypes were identified by PCR using a portion of each culture, as described elsewhere (34). For long term growth experiments, cells were cultured in the presence of either 3 or 20% O 2 and passaged every 4 days; mean population doublings were calculated from cell numbers.…”

Section: Transgenic Mice and Mef-we Generated Jdp2mentioning

confidence: 99%

“…For example, the overexpression of JDP2 inhibits the retinoic acid-dependent differentiation of embryonic carcinoma F9 cells (25). Recently, we generated JDP2-deficient (Jdp2-KO) mice and reported that mouse embryonic fibroblasts (MEFs), derived from Jdp2-KO mice (Jdp2 Ϫ/Ϫ MEF), were susceptible to adipocyte differentiation, suggesting that JDP2 might be involved in a signaling pathway for differentiation (34). In subsequent studies of Jdp2…”

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confidence: 99%

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JDP2 (Jun Dimerization Protein 2)-deficient Mouse Embryonic Fibroblasts Are Resistant to Replicative Senescence

Nakade

Pan

Yamasaki

et al. 2009

Journal of Biological Chemistry

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JDP2 (Jun dimerization protein 2, an AP-1 transcription factor) is involved in the regulation of the differentiation and proliferation of cells. We report here that JDP2-deficient mouse embryonic fibroblasts (Jdp2 ؊/؊ MEF) are resistant to replicative senescence. In the absence of JDP2, the level of expression of p16 Ink4a , which is known to rise as normal fibroblasts age, fell significantly when cells were cultured for more than 2 months. Conversely, the overexpression of JDP2 induced the expression of genes for p16Ink4a and p19 Arf . Moreover, at the promoter of the gene for p16Ink4a in Jdp2 ؊/؊ MEF, the extent of methylation of lysine 27 of histone H3 (H3K27), which is important for gene silencing, increased. Polycomb-repressive complexes (PRC-1 and PRC-2), which are responsible for histone methylation, bound efficiently to the promoter to repress the expression of the gene for p16Ink4a . As a result, JDP2-deficient MEF became resistant to replicative senescence. Our results indicate that JDP2 is involved in the signaling pathway for senescence via epigenetic regulation of the expression of the gene for p16Ink4a .

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“…It appears ubiquitously expressed and is involved in a variety of biological phenomena, such as cell differentiation (11)(12)(13)(14), apoptosis (15,16), and tumorigenesis (17)(18)(19)(20)(21)(22). It can dimerize, through its b-Zip motif, with itself or other b-Zip proteins, such as c-Jun, JunB, JunD, or ATF-2 (10,11,23), and function as a general repressor of, at least, AP-1, cAMP-response element, and TPA responsive element-dependent transcription (10,23).…”

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confidence: 99%

Involvement of Jun Dimerization Protein 2 (JDP2) in the Maintenance of Epstein-Barr Virus Latency

Murata

Noda

Saito

et al. 2011

Journal of Biological Chemistry

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Reactivation of the Epstein-Barr virus from latency is dependent on expression of the BZLF1 viral immediate-early protein.The BZLF1 promoter (Zp) normally exhibits only low basal activity but is activated in response to chemical inducers such as 12-O-tetradecanoylphorbol-13-acetate and calcium ionophore. We found that Jun dimerization protein 2 (JDP2) plays a significant role in suppressing Zp activity. Reporter, EMSA, and ChIP assays of a Zp mutant virus revealed JDP2 association with Zp at the ZII cis-element, a binding site for CREB/ATF/AP-1. Suppression of Zp activity by JDP2 correlated with HDAC3 association and reduced levels of histone acetylation. Although introduction of point mutations into the ZII element of the viral genome did not increase the level of BZLF1 production, silencing of endogenous JDP2 gene expression by RNA interference increased the levels of viral early gene products and viral DNA replication. These results indicate that JDP2 plays a role as a repressor of Zp and that its replacement by CREB/ ATF/AP-1 at ZII is crucial to triggering reactivation from latency to lytic replication.The Epstein-Barr virus (EBV) 2 is a human ␥-herpesvirus that predominantly establishes latent infection in B lymphocytes. Only a small percentage of infected cells switch from the latent stage into the lytic cycle to produce progeny viruses. Although the mechanism of EBV reactivation in vivo is not fully understood, it is known to be elicited by treatment of latently infected B cells with chemical or biological reagents, such as 12-O-tetradecanoylphorbol 13-acetate (TPA), calcium ionophore, sodium butyrate, or anti-immunoglobulin, at least in cultured cells. Stimulation of the EBV lytic cascade by any of these leads to expression of two immediate-early genes, BZLF1 and BRLF1.The BZLF1 protein is a transcriptional activator that shares structural similarities to basic leucine zipper (b-Zip) family transcriptional factors and acts as an oriLyt binding protein essential for lytic viral DNA replication. BZLF1 expression alone can trigger the entire reactivation cascade (1-3).Expression of the BZLF1 gene is tightly controlled at the transcriptional level. The BZLF1 promoter (Zp) normally exhibits low basal activity and is activated in response to TPA or the other reagents described above. The minimal sequence of Zp necessary for activation by the inducers is 233 bp in length (4). The region harbors at least three types of cis regulatory elements, referred to as ZI, ZII, and ZIII. Four copies of the ZI element (ZIA-D) are distributed within the minimal Zp. The myocyte enhancer factor 2D binds to ZIA, ZIB, and ZID (5), whereas Sp1 or Sp3 can bind to ZIA, ZIC, and ZID (6). A single ZII element is located near TATA, sharing homology with binding sites for the cyclic AMP-response element-binding protein (CREB), activating transcription factor (ATF), and activator protein-1 (AP-1) family transcriptional factors such as JunB and JunD (7,8). Two copies of the ZIII element (ZIII-A and -B) bind to the BZLF1 protein. Previou...

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JDP2 suppresses adipocyte differentiation by regulating histone acetylation

Cited by 52 publications

References 37 publications

IRF2‐binding protein‐1 is a JDP2 ubiquitin ligase and an inhibitor of ATF2‐dependent transcription

IRF2‐binding protein‐1 is a JDP2 ubiquitin ligase and an inhibitor of ATF2‐dependent transcription

JDP2 (Jun Dimerization Protein 2)-deficient Mouse Embryonic Fibroblasts Are Resistant to Replicative Senescence

Involvement of Jun Dimerization Protein 2 (JDP2) in the Maintenance of Epstein-Barr Virus Latency

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