Jun dimerization protein

Last updated
JDP2
Identifiers
Aliases JDP2 , JUNDM2, Jun dimerization protein 2
External IDs OMIM: 608657 MGI: 1932093 HomoloGene: 12787 GeneCards: JDP2
Orthologs
SpeciesHumanMouse
Entrez

122953

81703

Ensembl

ENSG00000140044

ENSMUSG00000034271

UniProt

Q8WYK2

P97875

RefSeq (mRNA)

NM_001135047
NM_001135048
NM_001135049
NM_130469

NM_001205052
NM_001205053
NM_030887
NM_001401266

RefSeq (protein)

NP_001128519
NP_001128520
NP_001128521
NP_569736

NP_001191981
NP_001191982
NP_112149
NP_001388195

Location (UCSC) Chr 14: 75.43 – 75.47 Mb Chr 12: 85.65 – 85.69 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Jun dimerization protein 2 (JUNDM2) is a protein that in humans is encoded by the JDP2 gene. [5] [6] [7] The Jun dimerization protein is a member of the AP-1 family of transcription factors. [5]

Contents

JDP 2 was found by a Sos-recruitment system,[ clarification needed ] to dimerize with c-Jun to repress AP-1-mediated activation. [5] It was later identified by the yeast-two hybrid system to bind to activating transcription factor 2 (ATF2) to repress ATF-mediated transcriptional activation. [8] JDP2 regulates 12-O-tetradecanoylphorbol-13-acetate (TPA) response element (TRE)- and cAMP-responsive element (CRE)-dependent transcription. [9]

The JDP2 gene is located on human chromosome 14q24.3 (46.4 kb, 75,427,715 bp to 75,474,111 bp) and mouse chromosome 12 (39 kb, 85,599,105 bp to 85,639,878 bp), [10] [11] which is located at about 250 kbp in the Fos-JDP2-BATF locus. [12] Alternative splicing of JDP2 generates at least two isoforms. [12] [13] The protein JDP2 has 163 amino acids, belongs to the family of basic leucine zipper (bZIP), and shows high homology with the ATF3 bZIP domain. [5] [14] The bZIP domain includes the amino acids from position 72 to 135, the basic motif from position 74 to 96, and the leucine zipper from 100 to 128. The molecular weight of the canonical JDP2 is 18,704 Da. The histone-binding region is located from position 35 to 72 and the inhibition of the histone acetyltransferase (INHAT) region is from position 35 to 135, [15] which is located before the DNA-binding domain.

JDP2 is expressed ubiquitously but is detected mainly in the cerebellum, brain, lung, and testis. [16] [17] A JDP2 single nucleotide polymorphism (SNP) was detected in Japanese, Korean, and Dutch cohorts, and is associated with an increased risk of intracranial aneurysms. [18]

Posttranscriptional and post translational modifications

Phosphorylation of the threonine (Thr) residue at position 148 is mediated by c-Jun N-terminal kinase (MAPK8; JNK1) and p38 MAPK. [19] [20] Phosphorylated ATF2 inhibits the formation with JDP2 in vitro [21] while phosphorylated JDP2 undergoes proteosomal degradation. [22] It contains putative SUMO modification of lysine (Lys) residue at position 65, [11] and recruits interferon regulatory factor 2 binding protein 1 (IRF2BP1), which acts as an E3 ligase. [23] Phosphorylation of Thr at position 148 is detected in response to various stress conditions such as UV irradiation, oxidative stress, and anisomycin treatment or JDP2 is also regulated by other kinases such as p38 MAPK [20] and doublecortin like protein kinase. [24] Polyubiquitination of JDP2 protein is induced by IRF2BP1. [23] JDP2 displays histone-binding and histone-chaperone activity. [25] [26] and inhibition of p300/CBP induced histone acetylation (INHAT). [25] [26] JDP2 recruits histone deacetylases HDAC1 and HDAC2, [27] [28] HDAC6 [27] and HDAC3. [29] JDP2 has INHAT activity [15] and inhibits histone methylation in vitro. [30]

Function

Phenotypes of gene knockout and transgenic mice

Gene knockout mice have a shorter tail, are smaller, have low neutrophil count. [16] [31] and cell proliferation, and commit to cell cycle arrest because of AP-1 repression. [16] TransgenicJDP2 mice display atrial dilation [32] and myocardial hypertrophy. [33]

Dimer formation and interacting molecules

JDP2 functions as a transcription activator or repressor depending on the leucine zipper protein member it is associated with. JDP2 forms a homodimer or heterodimer with c-Jun, JUNB, JUND, Fra2, ATF2. [5] [8] [27] and acts as a general repressor. On the other hand, JDP2 form a stable heterodimer with CHOP10 to enhance TRE- but not CRE-dependent transcription. [34] [35] In addition, JDP2 has been shown to directly associate with the progesterone receptor (PR) and functionally acts as a coactivator of progesterone-dependent PR-mediated gene transcription. [36] [37] [38] Other proteins such as interferon regulatory factor-2-binding protein-1 (IRF2BP1). [23] CCAAT/enhancer-binding protein gamma (C/EBPγ), [39] HDAC3 and HDAC6 [27] [29] have also been demonstrated to associate with JDP2.

Cell differentiation

JDP2 plays a role in cell differentiation in several systems. Ectopic expression of JDP2 inhibits the retinoic acid-induced differentiation of F9 cells [29] and adipocyte differentiation. [40] By contrast, JDP2 induces terminal muscle cell differentiation in C2 myoblasts and reduces the tumorigenicity of rhabdomyosarcoma cells and restored their ability to differentiate into myotubes. [41] It is also reported that JDP2 plays an important role in the RANK-mediated osteoclast differentiation. [42] Further, JDP2 is involved in neutrophil differentiation [31] and transcription factor Tbx3-mediated osteoclastogenesis [43] for host defense and bone homeostasis. [31] Methylome mapping suggests that JDP2 plays a role in cell progenitor differentiation of megakaryocytes. [44]

Regulation of cell cycle and p53 signaling

JDP2 induces cell cycle arrest through cyclin D, [41] p53, and cyclin A [16] transcription, by increasing JUNB, JUND, and Fra2, and by decreasing c-JUN through the loss of p27kip1. [45] JDP2 downregulates p53 transcription, which promotes leukemogenesis. [46] Mouse p53 protein negatively regulates the JDP2 promoter in F9 cells [47] as part of the JDP2˗p53 autoregulatory circuit. By contrast, JDP2-knockout mice exhibit in downregulation of p53 and p21 proteins. [16]

Apoptosis and senescence

JDP2 appears to be involved in the inhibition of apoptosis. Depletion of JDP2 induces cell death similar to apoptosis. [48] A study also demonstrated that UV irradiation induces JDP2 expression, which in turn down-regulates expression of p53 and thereby protects cells from UV-mediated programmed cell death. [49] Heart-specific JDP2 overexpression protects cardiomyocytes against hypertrophic growth and TGFβ–induced apoptosis. [50] In other settings, JDP2 has been shown to play an important role in the regulation of cellular senescence. JDP2-deficient mouse embryonic fibroblasts are resistant to replicative senescence by recruiting polycomb-repressive complexes (PRC1 and PRC2) to the promoters at the p16Ink4a locus. [25] [30]

Oxidative stress and antioxidative response

The increased accumulation of intracellular reactive oxygen species (ROS) and 8-oxo-dGuo, one of the major products of DNA oxidation, and the reduced expression of several transcripts involved in ROS metabolism in Jdp2-deficient MEFs argue that JDP2 is required to hold ROS levels in check. [17] [51] [52] Furthermore, JDP2 binds directly to the antioxidant responsive element (ARE) core sequence, associates with Nrf2 and MafK (Nrf2–MafK) via basic leucine zipper domains, and increases DNA-binding activity of the Nrf2–MafK complex to the ARE and the transcription of ARE-dependent genes such as HO1 and NQO1. [52] Therefore, JDP2 functions as an integral component of the Nrf2–MafK complex to modulate antioxidant and detoxification programs.

Nuclear reprogramming

JDP2, which has been shown to regulate Wnt signaling pathway and prevent ROS production, [16] [17] may play roles in cell reprogramming. Indeed, a study demonstrated that DAOY medulloblastoma cells can be reprogrammed successfully by JDP2 and the defined factor OCT4 to become induced pluripotent stem cells (iPSC)-like cells. This iPSC-like cells expressed stem cell-like characteristics including alkaline phosphatase activity and some stem cell markers, including SSEA3, SSEA4 and Tra-1-60. [17] Later, another study also showed that JDP2 can substitute Oct4 to generate iPSCs with Klf4, Sox2 and Myc (KSM) or KS[ clarification needed ] from somatic cells. [53] Moreover, they showed that JDP2 anchors five non-Yamanaka factors (ID1, JHDM1B, LRH1, SALL4, and GLIS1) to reprogram mouse embryonic fibroblasts into iPSCs.

Oncogene or tumor suppressor gene

JDP2 may act as a double-edge sword in tumorigenesis. It is reported that JDP2 inhibits Ras-dependent cell transformation in NIH3T3 cells and tumor development in xenografts transplanted into SCID mice. [45] Constitutive expression of JDP2 in rhabdomyosarcoma cells reduced their tumorigenic characteristics. [41] On the other hand, JDP2 induces partial oncogenic transformation of chicken embryonic fibroblasts. [9] Studies using high throughput viral insertional mutagenesis analysis also revealed that JDP2 functions as an oncogene. [6] [12] [13] [46] [54] [55] JDP2-transgenic mice display potentiation of liver cancer, higher mortality and increase number and size of tumors, especially when JDP2 expression is at the promotion stage. [56]

Cancer and disease markers

JDP2 shows the gene amplification of head and neck squamous-cell carcinoma. [57] In pancreatic carcinoma, downregulation of JDP2 is correlated with lymph node metastasis and distant metastasis and strongly associated with the post-surgery survival time, indicating that JDP2 may serve as a biomarker to predict the prognosis of patients with pancreatic cancer. [58] In addition, JDP2 overexpression reverses the epithelial-to-mesenchymal transition (EMT) induced by co-treatment with TGF-β1 and EGF in human pancreatic BxPC-3 cells, suggesting that JDP2 may be a molecular target for pancreatic carcinoma intervention. [59] Furthermore, it has been shown that the expression level of JDP2 gene upon acute myocardial infarction (AMI) is highly specific and a sensitive biomarker for predicting heart failure. [60] In T cell acute lymphoblastic leukaemia, JDP2 regulates pro-survival signalling through direct transcriptional regulation of MCL1 and leads to steroid resistance in vivo. [61]

JDP2 targets and JDP2-regulated genes

JDP2 is involved in the modulation of gene expression. For example, JDP2 regulates MyoD gene expression with c-Jun [41] and gene for galectin-7. [62] JDP2 functionally associated with HDAC3 and acts as a repressor to inhibit the amino acid regulation of CHOP transcription. [34] JDP2 and ATF3 are involved in recruiting HDACs to the ATF3 promoter region resulting in transcriptional repression of ATF3. [27] JDP2 inhibits the promoter of the Epstein–Barr virus (EBV) immediate early gene BZLF1 for the regulation of the latent-lytic switch in EBV infection. [63]

Interactions

JDP2 (gene) has been shown to interact with Activating transcription factor 2. [21]

Notes

Related Research Articles

<span class="mw-page-title-main">EP300</span> Protein-coding gene in the species Homo sapiens

Histone acetyltransferase p300 also known as p300 HAT or E1A-associated protein p300 also known as EP300 or p300 is an enzyme that, in humans, is encoded by the EP300 gene. It functions as histone acetyltransferase that regulates transcription of genes via chromatin remodeling by allowing histone proteins to wrap DNA less tightly. This enzyme plays an essential role in regulating cell growth and division, prompting cells to mature and assume specialized functions (differentiate), and preventing the growth of cancerous tumors. The p300 protein appears to be critical for normal development before and after birth.

<span class="mw-page-title-main">Transcription factor Sp1</span> Protein-coding gene in the species Homo sapiens

Transcription factor Sp1, also known as specificity protein 1* is a protein that in humans is encoded by the SP1 gene.

In molecular genetics, the Krüppel-like family of transcription factors (KLFs) are a set of eukaryotic C2H2 zinc finger DNA-binding proteins that regulate gene expression. This family has been expanded to also include the Sp transcription factor and related proteins, forming the Sp/KLF family.

<span class="mw-page-title-main">Protein c-Fos</span> Mammalian protein found in Homo sapiens

Protein c-Fos is a proto-oncogene that is the human homolog of the retroviral oncogene v-fos. It is encoded in humans by the FOS gene. It was first discovered in rat fibroblasts as the transforming gene of the FBJ MSV. It is a part of a bigger Fos family of transcription factors which includes c-Fos, FosB, Fra-1 and Fra-2. It has been mapped to chromosome region 14q21→q31. c-Fos encodes a 62 kDa protein, which forms heterodimer with c-jun, resulting in the formation of AP-1 complex which binds DNA at AP-1 specific sites at the promoter and enhancer regions of target genes and converts extracellular signals into changes of gene expression. It plays an important role in many cellular functions and has been found to be overexpressed in a variety of cancers.

<span class="mw-page-title-main">Transcription factor Jun</span> Mammalian protein found in Homo sapiens

Transcription factor Jun is a protein that in humans is encoded by the JUN gene. c-Jun, in combination with protein c-Fos, forms the AP-1 early response transcription factor. It was first identified as the Fos-binding protein p39 and only later rediscovered as the product of the JUN gene. c-jun was the first oncogenic transcription factor discovered. The proto-oncogene c-Jun is the cellular homolog of the viral oncoprotein v-jun. The viral homolog v-jun was discovered in avian sarcoma virus 17 and was named for ju-nana, the Japanese word for 17. The human JUN encodes a protein that is highly similar to the viral protein, which interacts directly with specific target DNA sequences to regulate gene expression. This gene is intronless and is mapped to 1p32-p31, a chromosomal region involved in both translocations and deletions in human malignancies.

<span class="mw-page-title-main">AP-1 transcription factor</span> Instance of defined set in Homo sapiens with Reactome ID (R-HSA-6806560)

Activator protein 1 (AP-1) is a transcription factor that regulates gene expression in response to a variety of stimuli, including cytokines, growth factors, stress, and bacterial and viral infections. AP-1 controls a number of cellular processes including differentiation, proliferation, and apoptosis. The structure of AP-1 is a heterodimer composed of proteins belonging to the c-Fos, c-Jun, ATF and JDP families.

<span class="mw-page-title-main">JunD</span> Protein-coding gene in the species Homo sapiens

Transcription factor JunD is a protein that in humans is encoded by the JUND gene.

<span class="mw-page-title-main">ATF3</span> Protein-coding gene in the species Homo sapiens

Cyclic AMP-dependent transcription factor ATF-3 is a protein that, in humans, is encoded by the ATF3 gene.

<span class="mw-page-title-main">TRIM28</span> Protein-coding gene in the species Homo sapiens

Tripartite motif-containing 28 (TRIM28), also known as transcriptional intermediary factor 1β (TIF1β) and KAP1, is a protein that in humans is encoded by the TRIM28 gene.

<span class="mw-page-title-main">PIAS4</span> Protein-coding gene in the species Homo sapiens

E3 SUMO-protein ligase PIAS4 is one of several protein inhibitor of activated STAT (PIAS) proteins. It is also known as protein inhibitor of activated STAT protein gamma, and is an enzyme that in humans is encoded by the PIAS4 gene.

<span class="mw-page-title-main">CTBP1</span> Protein-coding gene in the species Homo sapiens

C-terminal-binding protein 1 also known as CtBP1 is a protein that in humans is encoded by the CTBP1 gene. CtBP1 is one of two CtBP proteins, the other protein being CtBP2.

<span class="mw-page-title-main">PIAS1</span> Protein-coding gene in the species Homo sapiens

E3 SUMO-protein ligase PIAS1 is an enzyme that in humans is encoded by the PIAS1 gene.

<span class="mw-page-title-main">Histone deacetylase 5</span> Protein-coding gene in the species Homo sapiens

Histone deacetylase 5 is an enzyme that in humans is encoded by the HDAC5 gene.

<span class="mw-page-title-main">HDAC9</span> Protein-coding gene in the species Homo sapiens

Histone deacetylase 9 is an enzyme that in humans is encoded by the HDAC9 gene.

<span class="mw-page-title-main">ZNF148</span> Gene of the species Homo sapiens

Zinc finger protein 148 is a protein that in humans is encoded by the ZNF148 gene.

<span class="mw-page-title-main">HEY2</span> Protein-coding gene in the species Homo sapiens

Hairy/enhancer-of-split related with YRPW motif protein 2 (HEY2) also known as cardiovascular helix-loop-helix factor 1 (CHF1) is a protein that in humans is encoded by the HEY2 gene.

<span class="mw-page-title-main">MXD1</span> Protein-coding gene in the species Homo sapiens

MAD protein is a protein that in humans is encoded by the MXD1 gene.

<span class="mw-page-title-main">Retinoblastoma protein</span> Mammalian protein found in Homo sapiens

The retinoblastoma protein is a tumor suppressor protein that is dysfunctional in several major cancers. One function of pRb is to prevent excessive cell growth by inhibiting cell cycle progression until a cell is ready to divide. When the cell is ready to divide, pRb is phosphorylated, inactivating it, and the cell cycle is allowed to progress. It is also a recruiter of several chromatin remodeling enzymes such as methylases and acetylases.

<span class="mw-page-title-main">KLF15</span> Protein-coding gene in the species Homo sapiens

Krüppel-like factor 15 is a protein that in humans is encoded by the KLF15 gene in the Krüppel-like factor family. Its former designation KKLF stands for kidney-enriched Krüppel-like factor.

<span class="mw-page-title-main">EHMT1</span> Protein-coding gene in the species Homo sapiens

Euchromatic histone-lysine N-methyltransferase 1, also known as G9a-like protein (GLP), is a protein that in humans is encoded by the EHMT1 gene.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000140044 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000034271 - Ensembl, May 2017
  3. ↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. 1 2 3 4 5 Aronheim A, Zandi E, Hennemann H, Elledge SJ, Karin M (June 1997). "Isolation of an AP-1 repressor by a novel method for detecting protein-protein interactions". Molecular and Cellular Biology. 17 (6): 3094–3102. doi:10.1128/mcb.17.6.3094. PMC   232162 . PMID   9154808.
  6. 1 2 Stewart M, Mackay N, Hanlon L, Blyth K, Scobie L, Cameron E, Neil JC (June 2007). "Insertional mutagenesis reveals progression genes and checkpoints in MYC/Runx2 lymphomas". Cancer Research. 67 (11): 5126–5133. doi:10.1158/0008-5472.CAN-07-0433. PMC   2562448 . PMID   17545590.
  7. ↑ "Entrez Gene: JDP2 jun dimerization protein 2".
  8. 1 2 Jin C, Ugai H, Song J, Murata T, Nili F, Sun K, et al. (January 2001). "Identification of mouse Jun dimerization protein 2 as a novel repressor of ATF-2". FEBS Letters. 489 (1): 34–41. doi: 10.1016/s0014-5793(00)02387-5 . PMID   11231009. S2CID   43837367.
  9. 1 2 Blazek E, Wasmer S, Kruse U, Aronheim A, Aoki M, Vogt PK (April 2003). "Partial oncogenic transformation of chicken embryo fibroblasts by Jun dimerization protein 2, a negative regulator of TRE- and CRE-dependent transcription". Oncogene. 22 (14): 2151–2159. doi: 10.1038/sj.onc.1206312 . PMID   12687017.
  10. ↑ GeneCard for JDP2
  11. 1 2 Universal protein resource accession number Q8WYK2 at UniProt.
  12. 1 2 3 Rasmussen MH, Sørensen AB, Morris DW, Dutra JC, Engelhard EK, Wang CL, et al. (July 2005). "Tumor model-specific proviral insertional mutagenesis of the Fos/Jdp2/Batf locus". Virology. 337 (2): 353–364. doi: 10.1016/j.virol.2005.04.027 . PMID   15913695.
  13. 1 2 Rasmussen MH, Wang B, Wabl M, Nielsen AL, Pedersen FS (August 2009). "Activation of alternative Jdp2 promoters and functional protein isoforms in T-cell lymphomas by retroviral insertion mutagenesis". Nucleic Acids Research. 37 (14): 4657–4671. doi:10.1093/nar/gkp469. PMC   2724284 . PMID   19502497.
  14. ↑ Weidenfeld-Baranboim K, Hasin T, Darlyuk I, Heinrich R, Elhanani O, Pan J, et al. (April 2009). "The ubiquitously expressed bZIP inhibitor, JDP2, suppresses the transcription of its homologue immediate early gene counterpart, ATF3". Nucleic Acids Research. 37 (7): 2194–2203. doi:10.1093/nar/gkp083. PMC   2673429 . PMID   19233874.
  15. 1 2 Jin C, Kato K, Chimura T, Yamasaki T, Nakade K, Murata T, et al. (April 2006). "Regulation of histone acetylation and nucleosome assembly by transcription factor JDP2". Nature Structural & Molecular Biology. 13 (4): 331–338. doi:10.1038/nsmb1063. PMID   16518400. S2CID   21957070.
  16. 1 2 3 4 5 6 Pan J, Nakade K, Huang YC, Zhu ZW, Masuzaki S, Hasegawa H, et al. (November 2010). "Suppression of cell-cycle progression by Jun dimerization protein-2 (JDP2) involves downregulation of cyclin-A2". Oncogene. 29 (47): 6245–6256. doi:10.1038/onc.2010.355. PMC   3007677 . PMID   20802531.
  17. 1 2 3 4 Chiou SS, Wang SS, Wu DC, Lin YC, Kao LP, Kuo KK, et al. (July 2013). "Control of Oxidative Stress and Generation of Induced Pluripotent Stem Cell-like Cells by Jun Dimerization Protein 2". Cancers. 5 (3): 959–984. doi: 10.3390/cancers5030959 . PMC   3795374 . PMID   24202329.
  18. ↑ Krischek B, Tajima A, Akagawa H, Narita A, Ruigrok Y, Rinkel G, et al. (August 2010). "Association of the Jun dimerization protein 2 gene with intracranial aneurysms in Japanese and Korean cohorts as compared to a Dutch cohort". Neuroscience. 169 (1): 339–343. doi:10.1016/j.neuroscience.2010.05.002. PMID   20452405. S2CID   28550508.
  19. ↑ Katz S, Heinrich R, Aronheim A (October 2001). "The AP-1 repressor, JDP2, is a bona fide substrate for the c-Jun N-terminal kinase". FEBS Letters. 506 (3): 196–200. doi: 10.1016/s0014-5793(01)02907-6 . PMID   11602244. S2CID   43077117.
  20. 1 2 Katz S, Aronheim A (December 2002). "Differential targeting of the stress mitogen-activated protein kinases to the c-Jun dimerization protein 2". The Biochemical Journal. 368 (Pt 3): 939–945. doi:10.1042/BJ20021127. PMC   1223036 . PMID   12225289.
  21. 1 2 Murata T, Shinozuka Y, Obata Y, Yokoyama KK (May 2008). "Phosphorylation of two eukaryotic transcription factors, Jun dimerization protein 2 and activation transcription factor 2, in Escherichia coli by Jun N-terminal kinase 1". Analytical Biochemistry. 376 (1): 115–121. doi:10.1016/j.ab.2008.01.038. PMID   18307971.
  22. ↑ Weidenfeld-Baranboim K, Koren L, Aronheim A (June 2011). "Phosphorylation of JDP2 on threonine-148 by the c-Jun N-terminal kinase targets it for proteosomal degradation". The Biochemical Journal. 436 (3): 661–669. doi:10.1042/BJ20101031. PMID   21463260. S2CID   11422858.
  23. 1 2 3 Kimura M (August 2008). "IRF2-binding protein-1 is a JDP2 ubiquitin ligase and an inhibitor of ATF2-dependent transcription". FEBS Letters. 582 (19): 2833–2837. doi: 10.1016/j.febslet.2008.07.033 . PMID   18671972. S2CID   5226333.
  24. ↑ Nagamine T, Nomada S, Onouchi T, Kameshita I, Sueyoshi N (March 2014). "Nuclear translocation of doublecortin-like protein kinase and phosphorylation of a transcription factor JDP2". Biochemical and Biophysical Research Communications. 446 (1): 73–78. doi:10.1016/j.bbrc.2014.02.075. PMID   24582561.
  25. 1 2 3 Huang YC, Saito S, Yokoyama KK (October 2010). "Histone chaperone Jun dimerization protein 2 (JDP2): role in cellular senescence and aging". The Kaohsiung Journal of Medical Sciences. 26 (10): 515–531. doi: 10.1016/S1607-551X(10)70081-4 . PMID   20950777.
  26. 1 2 Pan J, Jin C, Murata T, Yokoyama KK (2003). "Sequence specific transcription factor, JDP2 interacts with histone and inhibits p300-mediated histone acetylation". Nucleic Acids Research. Supplement. 3 (3): 305–306. doi: 10.1093/nass/3.1.305 . PMID   14510502.
  27. 1 2 3 4 5 Darlyuk-Saadon I, Weidenfeld-Baranboim K, Yokoyama KK, Hai T, Aronheim A (2012). "The bZIP repressor proteins, c-Jun dimerization protein 2 and activating transcription factor 3, recruit multiple HDAC members to the ATF3 promoter". Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms. 1819 (11–12): 1142–1153. doi:10.1016/j.bbagrm.2012.09.005. PMC   3551276 . PMID   22989952.
  28. ↑ Heideman MR, Wilting RH, Yanover E, Velds A, de Jong J, Kerkhoven RM, et al. (March 2013). "Dosage-dependent tumor suppression by histone deacetylases 1 and 2 through regulation of c-Myc collaborating genes and p53 function". Blood. 121 (11): 2038–2050. doi:10.1182/blood-2012-08-450916. PMC   3596963 . PMID   23327920.
  29. 1 2 3 Jin C, Li H, Murata T, Sun K, Horikoshi M, Chiu R, Yokoyama KK (July 2002). "JDP2, a repressor of AP-1, recruits a histone deacetylase 3 complex to inhibit the retinoic acid-induced differentiation of F9 cells". Molecular and Cellular Biology. 22 (13): 4815–4826. doi:10.1128/mcb.22.13.4815-4826.2002. PMC   133911 . PMID   12052888.
  30. 1 2 Nakade K, Pan J, Yamasaki T, Murata T, Wasylyk B, Yokoyama KK (April 2009). "JDP2 (Jun Dimerization Protein 2)-deficient mouse embryonic fibroblasts are resistant to replicative senescence". The Journal of Biological Chemistry. 284 (16): 10808–10817. doi: 10.1074/jbc.M808333200 . PMC   2667768 . PMID   19233846.
  31. 1 2 3 Maruyama K, Fukasaka M, Vandenbon A, Saitoh T, Kawasaki T, Kondo T, et al. (December 2012). "The transcription factor Jdp2 controls bone homeostasis and antibacterial immunity by regulating osteoclast and neutrophil differentiation". Immunity. 37 (6): 1024–1036. doi: 10.1016/j.immuni.2012.08.022 . PMID   23200825.
  32. ↑ Kehat I, Heinrich R, Ben-Izhak O, Miyazaki H, Gutkind JS, Aronheim A (June 2006). "Inhibition of basic leucine zipper transcription is a major mediator of atrial dilatation". Cardiovascular Research. 70 (3): 543–554. doi: 10.1016/j.cardiores.2006.02.018 . PMID   16631626.
  33. ↑ Kehat I, Hasin T, Aronheim A (October 2006). "The role of basic leucine zipper protein-mediated transcription in physiological and pathological myocardial hypertrophy". Annals of the New York Academy of Sciences. 1080 (1): 97–109. Bibcode:2006NYASA1080...97K. doi:10.1196/annals.1380.009. PMID   17132778. S2CID   19775029.
  34. 1 2 Chérasse Y, Chaveroux C, Jousse C, Maurin AC, Carraro V, Parry L, et al. (April 2008). "Role of the repressor JDP2 in the amino acid-regulated transcription of CHOP". FEBS Letters. 582 (10): 1537–1541. doi:10.1016/j.febslet.2008.03.050. PMID   18396163. S2CID   8438516.
  35. ↑ Weidenfeld-Baranboim K, Bitton-Worms K, Aronheim A (June 2008). "TRE-dependent transcription activation by JDP2-CHOP10 association". Nucleic Acids Research. 36 (11): 3608–3619. doi:10.1093/nar/gkn268. PMC   2441799 . PMID   18463134.
  36. ↑ Hill KK, Roemer SC, Jones DN, Churchill ME, Edwards DP (September 2009). "A progesterone receptor co-activator (JDP2) mediates activity through interaction with residues in the carboxyl-terminal extension of the DNA binding domain". The Journal of Biological Chemistry. 284 (36): 24415–24424. doi: 10.1074/jbc.M109.003244 . PMC   2782034 . PMID   19553667.
  37. ↑ Wardell SE, Boonyaratanakornkit V, Adelman JS, Aronheim A, Edwards DP (August 2002). "Jun dimerization protein 2 functions as a progesterone receptor N-terminal domain coactivator". Molecular and Cellular Biology. 22 (15): 5451–5466. doi:10.1128/mcb.22.15.5451-5466.2002. PMC   133955 . PMID   12101239.
  38. ↑ Edwards DP, Wardell SE, Boonyaratanakornkit V (December 2002). "Progesterone receptor interacting coregulatory proteins and cross talk with cell signaling pathways". The Journal of Steroid Biochemistry and Molecular Biology. 83 (1–5): 173–186. doi:10.1016/s0960-0760(02)00265-0. PMID   12650714. S2CID   22258908.
  39. ↑ Broder YC, Katz S, Aronheim A (October 1998). "The ras recruitment system, a novel approach to the study of protein-protein interactions". Current Biology. 8 (20): 1121–1124. doi: 10.1016/s0960-9822(98)70467-1 . PMID   9778531. S2CID   16085672.
  40. ↑ Nakade K, Pan J, Yoshiki A, Ugai H, Kimura M, Liu B, et al. (August 2007). "JDP2 suppresses adipocyte differentiation by regulating histone acetylation". Cell Death and Differentiation. 14 (8): 1398–1405. doi: 10.1038/sj.cdd.4402129 . PMID   17464331.
  41. 1 2 3 4 Ostrovsky O, Bengal E, Aronheim A (October 2002). "Induction of terminal differentiation by the c-Jun dimerization protein JDP2 in C2 myoblasts and rhabdomyosarcoma cells". The Journal of Biological Chemistry. 277 (42): 40043–40054. doi: 10.1074/jbc.M205494200 . PMID   12171923.
  42. ↑ Kawaida R, Ohtsuka T, Okutsu J, Takahashi T, Kadono Y, Oda H, et al. (April 2003). "Jun dimerization protein 2 (JDP2), a member of the AP-1 family of transcription factor, mediates osteoclast differentiation induced by RANKL". The Journal of Experimental Medicine. 197 (8): 1029–1035. doi:10.1084/jem.20021321. PMC   2193879 . PMID   12707301.
  43. ↑ Yao C, Yao GQ, Sun BH, Zhang C, Tommasini SM, Insogna K (March 2014). "The transcription factor T-box 3 regulates colony-stimulating factor 1-dependent Jun dimerization protein 2 expression and plays an important role in osteoclastogenesis". The Journal of Biological Chemistry. 289 (10): 6775–6790. doi: 10.1074/jbc.M113.499210 . PMC   3945339 . PMID   24394418.
  44. ↑ Ji H, Ehrlich LI, Seita J, Murakami P, Doi A, Lindau P, et al. (September 2010). "Comprehensive methylome map of lineage commitment from haematopoietic progenitors". Nature. 467 (7313): 338–342. Bibcode:2010Natur.467..338J. doi:10.1038/nature09367. PMC   2956609 . PMID   20720541.
  45. 1 2 Heinrich R, Livne E, Ben-Izhak O, Aronheim A (February 2004). "The c-Jun dimerization protein 2 inhibits cell transformation and acts as a tumor suppressor gene". The Journal of Biological Chemistry. 279 (7): 5708–5715. doi: 10.1074/jbc.M307608200 . PMID   14627710.
  46. 1 2 van der Weyden L, Rust AG, McIntyre RE, Robles-Espinoza CD, del Castillo Velasco-Herrera M, Strogantsev R, et al. (January 2013). "Jdp2 downregulates Trp53 transcription to promote leukaemogenesis in the context of Trp53 heterozygosity". Oncogene. 32 (3): 397–402. doi:10.1038/onc.2012.56. PMC   3550594 . PMID   22370638.
  47. ↑ Xu Y, Jin C, Liu Z, Pan J, Li H, Zhang Z, et al. (August 2014). "Cloning and characterization of the mouse JDP2 gene promoter reveal negative regulation by p53". Biochemical and Biophysical Research Communications. 450 (4): 1531–1536. doi: 10.1016/j.bbrc.2014.07.034 . PMID   25026555.
  48. ↑ Lerdrup M, Holmberg C, Dietrich N, Shaulian E, Herdegen T, Jäättelä M, Kallunki T (August 2005). "Depletion of the AP-1 repressor JDP2 induces cell death similar to apoptosis". Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1745 (1): 29–37. doi:10.1016/j.bbamcr.2005.06.008. PMID   16026868.
  49. ↑ Piu F, Aronheim A, Katz S, Karin M (May 2001). "AP-1 repressor protein JDP-2: inhibition of UV-mediated apoptosis through p53 down-regulation". Molecular and Cellular Biology. 21 (9): 3012–3024. doi:10.1128/MCB.21.9.3012-3024.2001. PMC   86930 . PMID   11287607.
  50. ↑ Hill C, Würfel A, Heger J, Meyering B, Schlüter KD, Weber M, et al. (July 2013). "Inhibition of AP-1 signaling by JDP2 overexpression protects cardiomyocytes against hypertrophy and apoptosis induction". Cardiovascular Research. 99 (1): 121–128. doi: 10.1093/cvr/cvt094 . PMID   23612584.
  51. ↑ Wang SW, Lee JK, Ku CC, Chiou SS, Steve Lin CL, Ho MF, et al. (2011). "Jun dimerization protein 2 in oxygen restriction; control of senescence". Current Pharmaceutical Design. 17 (22): 2278–2289. doi:10.2174/138161211797052394. PMID   21736542.
  52. 1 2 Tanigawa S, Lee CH, Lin CS, Ku CC, Hasegawa H, Qin S, et al. (November 2013). "Jun dimerization protein 2 is a critical component of the Nrf2/MafK complex regulating the response to ROS homeostasis". Cell Death & Disease. 4 (11): e921. doi:10.1038/cddis.2013.448. PMC   3847324 . PMID   24232097.
  53. ↑ Liu J, Han Q, Peng T, Peng M, Wei B, Li D, et al. (July 2015). "The oncogene c-Jun impedes somatic cell reprogramming". Nature Cell Biology. 17 (7): 856–867. doi:10.1038/ncb3193. PMID   26098572. S2CID   24437051.
  54. ↑ Hwang HC, Martins CP, Bronkhorst Y, Randel E, Berns A, Fero M, Clurman BE (August 2002). "Identification of oncogenes collaborating with p27Kip1 loss by insertional mutagenesis and high-throughput insertion site analysis". Proceedings of the National Academy of Sciences of the United States of America. 99 (17): 11293–11298. Bibcode:2002PNAS...9911293H. doi: 10.1073/pnas.162356099 . PMC   123250 . PMID   12151601.
  55. ↑ Rasmussen MH, Ballarín-González B, Liu J, Lassen LB, Füchtbauer A, Füchtbauer EM, et al. (April 2010). "Antisense transcription in gammaretroviruses as a mechanism of insertional activation of host genes". Journal of Virology. 84 (8): 3780–3788. doi:10.1128/JVI.02088-09. PMC   2849499 . PMID   20130045.
  56. ↑ Bitton-Worms K, Pikarsky E, Aronheim A (March 2010). "The AP-1 repressor protein, JDP2, potentiates hepatocellular carcinoma in mice". Molecular Cancer. 9: 54. doi: 10.1186/1476-4598-9-54 . PMC   2841123 . PMID   20214788.
  57. ↑ Järvinen AK, Autio R, Kilpinen S, Saarela M, Leivo I, Grénman R, et al. (June 2008). "High-resolution copy number and gene expression microarray analyses of head and neck squamous cell carcinoma cell lines of tongue and larynx". Genes, Chromosomes & Cancer. 47 (6): 500–509. doi:10.1002/gcc.20551. PMID   18314910. S2CID   9442226.
  58. ↑ Yuanhong X, Feng X, Qingchang L, Jianpeng F, Zhe L, Kejian G (2009). "Downregulation of AP-1 repressor JDP2 is associated with tumor metastasis and poor prognosis in patients with pancreatic carcinoma". The International Journal of Biological Markers. 25 (3): 136–140. doi:10.1177/172460081002500303. PMID   20677166. S2CID   208044673.
  59. ↑ Liu Z, Du R, Long J, Dong A, Fan J, Guo K, Xu Y (October 2012). "JDP2 inhibits the epithelial-to-mesenchymal transition in pancreatic cancer BxPC3 cells". Tumour Biology. 33 (5): 1527–1534. doi:10.1007/s13277-012-0404-5. PMID   22535371. S2CID   15934564.
  60. ↑ Maciejak A, Kiliszek M, Michalak M, Tulacz D, Opolski G, Matlak K, et al. (2015). "Gene expression profiling reveals potential prognostic biomarkers associated with the progression of heart failure". Genome Medicine. 7 (1): 26. doi: 10.1186/s13073-015-0149-z . PMC   4432772 . PMID   25984239.
  61. ↑ Mansour MR, He S, Li Z, Lobbardi R, Abraham BJ, Hug C, et al. (July 2018). "JDP2: An oncogenic bZIP transcription factor in T cell acute lymphoblastic leukemia". The Journal of Experimental Medicine. 215 (7): 1929–1945. doi:10.1084/jem.20170484. PMC   6028512 . PMID   29941549.
  62. ↑ Barkan B, Cox AD, Kloog Y (February 2013). "Ras inhibition boosts galectin-7 at the expense of galectin-1 to sensitize cells to apoptosis". Oncotarget. 4 (2): 256–268. doi:10.18632/oncotarget.844. PMC   3712571 . PMID   23530091.
  63. ↑ Murata T, Noda C, Saito S, Kawashima D, Sugimoto A, Isomura H, et al. (June 2011). "Involvement of Jun dimerization protein 2 (JDP2) in the maintenance of Epstein-Barr virus latency". The Journal of Biological Chemistry. 286 (25): 22007–22016. doi: 10.1074/jbc.M110.199836 . PMC   3121345 . PMID   21525011.

Further reading

This page is based on this Wikipedia article
Text is available under the CC BY-SA 4.0 license; additional terms may apply.
Images, videos and audio are available under their respective licenses.