Jun dimerization protein

Revision as of 06:21, 10 January 2019 by Matt Pijoan (talk | contribs) (1 revision imported)
(diff) ← Older revision | Latest revision (diff) | Newer revision → (diff)
Jump to navigation Jump to search
VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

n/a

n/a

Ensembl

n/a

n/a

UniProt

n/a

n/a

RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Jun dimerization protein 2 (JUNDM2) is a protein that in humans is encoded by the JDP2 gene.[1][2][3] The Jun dimerization protein is a member of the AP-1 family of transcription factors.[1]

JDP 2 was found by a Sos-recruitment system,[clarification needed] to dimerize with c-Jun to repress AP-1-mediated activation.[1] It was later identified by the yeast-two hybrid system to bind to activating transcription factor 2 (ATF2) to repress ATF-mediated transcriptional activation.[4] JDP2 regulates 12-O-tetradecanoylphorbol-13-acetate (TPA) response element (TRE)- and cAMP-responsive element (CRE)-dependent transcription.[5]

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),[6][7] which is located at about 250 kbp in the Fos-JDP2-BATF locus.[8] Alternative splicing of JDP2 generates at least two isoforms.[8][9] 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.[1][10] 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,[11] which is located before the DNA-binding domain.

JDP2 is expressed ubiquitously but is detected mainly in the cerebellum, brain, lung, and testis.[12][13] A JDP2 single nucleotide polymorphism (SNP) was detected in Japanese, Korean, and Dutch cohorts, and is associated with an increased risk of intracranial aneurysms.[14]

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.[15][16] Phosphorylated ATF2 inhibits the formation with JDP2 in vitro[17] while phosphorylated JDP2 undergoes proteosomal degradation.[18] It contains putative SUMO modification of lysine (Lys) residue at position 65,[7] and recruits interferon regulatory factor 2 binding protein 1 (IRF2BP1), which acts as an E3 ligase.[19] 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[16] and doublecortin like protein kinase.[20] Polyubiquitination of JDP2 protein is induced by IRF2BP1.[19] JDP2 displays histone-binding and histone-chaperone activity.[21][22] and inhibition of p300/CBP induced histone acetylation (INHAT).[21][22] JDP2 recruits histone deacetylases HDAC1 and HDAC2,[23][24] HDAC6[23] and HDAC3.[25] JDP2 has INHAT activity[11] and inhibits histone methylation in vitro.[26]

Function

Phenotypes of gene knockout and transgenic mice

Gene knockout mice have a shorter tail, are smaller, have low neutrophil count.[12][27] and cell proliferation, and commit to cell cycle arrest because of AP-1 repression.[12] TransgenicJDP2 mice display atrial dilation[28] and myocardial hypertrophy.[29]

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.[1][4][23] 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.[30][31] 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.[32][33][34] Other proteins such as interferon regulatory factor-2-binding protein-1 (IRF2BP1).[19] CCAAT/enhancer-binding protein gamma (C/EBPγ),[35] HDAC3 and HDAC6[23][25] 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[25] and adipocyte differentiation.[36] 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.[37] It is also reported that JDP2 plays an important role in the RANK-mediated osteoclast differentiation.[38] Further, JDP2 is involved in neutrophil differentiation[27] and transcription factor Tbx3-mediated osteoclastogenesis[39] for host defense and bone homeostasis.[27] Methylome mapping suggests that JDP2 plays a role in cell progenitor differentiation of megakaryocytes.[40]

Regulation of cell cycle and p53 signaling

JDP2 induces cell cycle arrest through cyclin D,[37] p53, and cyclin A[12] transcription, by increasing JUNB, JUND, and Fra2, and by decreasing c-JUN through the loss of p27kip1.[41] JDP2 downregulates p53 transcription, which promotes leukemogenesis.[42] Mouse p53 protein negatively regulates the JDP2 promoter in F9 cells[43] as part of the JDP2˗p53 autoregulatory circuit. By contrast, JDP2-knockout mice exhibit in downregulation of p53 and p21 proteins.[12]

Apoptosis and senescence

JDP2 appears to be involved in the inhibition of apoptosis. Depletion of JDP2 induces cell death similar to apoptosis.[44] 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.[45] Heart-specific JDP2 overexpression protects cardiomyocytes against hypertrophic growth and TGFβ–induced apoptosis.[46] 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.[21][26]

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.[13][47][48] 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.[48] 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,[12][13] 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.[13] 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.[49] 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.[41] Constitutive expression of JDP2 in rhabdomyosarcoma cells reduced their tumorigenic characteristics.[37] On the other hand, JDP2 induces partial oncogenic transformation of chicken embryonic fibroblasts.[5] Studies using high throughput viral insertional mutagenesis analysis also revealed that JDP2 functions as an oncogene.[2][8][9][42][50][51] 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.[52]

Cancer and disease markers

JDP2 shows the gene amplification of head and neck squamous-cell carcinoma.[53] 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.[54] 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.[55] 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.[56]

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[37] and gene for galectin-7.[57] JDP2 functionally associated with HDAC3 and acts as a repressor to inhibit the amino acid regulation of CHOP transcription.[30] JDP2 and ATF3 are involved in recruiting HDACs to the ATF3 promoter region resulting in transcriptional repression of ATF3.[23] 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.[58]

Interactions

JDP2 (gene) has been shown to interact with Activating transcription factor 2.[17]

References

  1. ↑ 1.0 1.1 1.2 1.3 1.4 Aronheim A, Zandi E, Hennemann H, Elledge SJ, Karin M (Jun 1997). "Isolation of an AP-1 repressor by a novel method for detecting protein-protein interactions". Molecular and Cellular Biology. 17 (6): 3094–102. doi:10.1128/mcb.17.6.3094. PMC 232162. PMID 9154808.
  2. ↑ 2.0 2.1 Stewart M, Mackay N, Hanlon L, Blyth K, Scobie L, Cameron E, Neil JC (Jun 2007). "Insertional mutagenesis reveals progression genes and checkpoints in MYC/Runx2 lymphomas". Cancer Research. 67 (11): 5126–33. doi:10.1158/0008-5472.CAN-07-0433. PMC 2562448. PMID 17545590.
  3. ↑ "Entrez Gene: JDP2 jun dimerization protein 2".
  4. ↑ 4.0 4.1 Jin C, Ugai H, Song J, Murata T, Nili F, Sun K, Horikoshi M, Yokoyama KK (Jan 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.
  5. ↑ 5.0 5.1 Blazek E, Wasmer S, Kruse U, Aronheim A, Aoki M, Vogt PK (Apr 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): 2151–9. doi:10.1038/sj.onc.1206312. PMID 12687017.
  6. ↑ GeneCard for JDP2
  7. ↑ 7.0 7.1 Universal protein resource accession number Q8WYK2 at UniProt.
  8. ↑ 8.0 8.1 8.2 Rasmussen MH, Sørensen AB, Morris DW, Dutra JC, Engelhard EK, Wang CL, Schmidt J, Pedersen FS (Jul 2005). "Tumor model-specific proviral insertional mutagenesis of the Fos/Jdp2/Batf locus". Virology. 337 (2): 353–64. doi:10.1016/j.virol.2005.04.027. PMID 15913695.
  9. ↑ 9.0 9.1 Rasmussen MH, Wang B, Wabl M, Nielsen AL, Pedersen FS (Aug 2009). "Activation of alternative Jdp2 promoters and functional protein isoforms in T-cell lymphomas by retroviral insertion mutagenesis". Nucleic Acids Research. 37 (14): 4657–71. doi:10.1093/nar/gkp469. PMC 2724284. PMID 19502497.
  10. ↑ Weidenfeld-Baranboim K, Hasin T, Darlyuk I, Heinrich R, Elhanani O, Pan J, Yokoyama KK, Aronheim A (Apr 2009). "The ubiquitously expressed bZIP inhibitor, JDP2, suppresses the transcription of its homologue immediate early gene counterpart, ATF3". Nucleic Acids Research. 37 (7): 2194–203. doi:10.1093/nar/gkp083. PMC 2673429. PMID 19233874.
  11. ↑ 11.0 11.1 Jin C, Kato K, Chimura T, Yamasaki T, Nakade K, Murata T, Li H, Pan J, Zhao M, Sun K, Chiu R, Ito T, Nagata K, Horikoshi M, Yokoyama KK (Apr 2006). "Regulation of histone acetylation and nucleosome assembly by transcription factor JDP2". Nature Structural & Molecular Biology. 13 (4): 331–8. doi:10.1038/nsmb1063. PMID 16518400.
  12. ↑ 12.0 12.1 12.2 12.3 12.4 12.5 Pan J, Nakade K, Huang YC, Zhu ZW, Masuzaki S, Hasegawa H, Murata T, Yoshiki A, Yamaguchi N, Lee CH, Yang WC, Tsai EM, Obata Y, Yokoyama KK (Nov 2010). "Suppression of cell-cycle progression by Jun dimerization protein-2 (JDP2) involves downregulation of cyclin-A2". Oncogene. 29 (47): 6245–56. doi:10.1038/onc.2010.355. PMC 3007677. PMID 20802531.
  13. ↑ 13.0 13.1 13.2 13.3 Chiou SS, Wang SS, Wu DC, Lin YC, Kao LP, Kuo KK, Wu CC, Chai CY, Lin CL, Lee CY, Liao YM, Wuputra K, Yang YH, Wang SW, Ku CC, Nakamura Y, Saito S, Hasegawa H, Yamaguchi N, Miyoshi H, Lin CS, Eckner R, Yokoyama KK (26 July 2013). "Control of Oxidative Stress and Generation of Induced Pluripotent Stem Cell-like Cells by Jun Dimerization Protein 2". Cancers. 5 (3): 959–84. doi:10.3390/cancers5030959. PMC 3795374. PMID 24202329.
  14. ↑ Krischek B, Tajima A, Akagawa H, Narita A, Ruigrok Y, Rinkel G, Wijmenga C, Feigl GC, Kim CJ, Hori T, Tatagiba M, Kasuya H, Inoue I (Aug 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): 339–43. doi:10.1016/j.neuroscience.2010.05.002. PMID 20452405.
  15. ↑ Katz S, Heinrich R, Aronheim A (Oct 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.
  16. ↑ 16.0 16.1 Katz S, Aronheim A (Dec 2002). "Differential targeting of the stress mitogen-activated protein kinases to the c-Jun dimerization protein 2". The Biochemical Journal. 368 (Pt 3): 939–45. doi:10.1042/BJ20021127. PMC 1223036. PMID 12225289.
  17. ↑ 17.0 17.1 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): 115–21. doi:10.1016/j.ab.2008.01.038. PMID 18307971.
  18. ↑ Weidenfeld-Baranboim K, Koren L, Aronheim A (Jun 2011). "Phosphorylation of JDP2 on threonine-148 by the c-Jun N-terminal kinase targets it for proteosomal degradation". The Biochemical Journal. 436 (3): 661–9. doi:10.1042/BJ20101031. PMID 21463260.
  19. ↑ 19.0 19.1 19.2 Kimura M (Aug 2008). "IRF2-binding protein-1 is a JDP2 ubiquitin ligase and an inhibitor of ATF2-dependent transcription". FEBS Letters. 582 (19): 2833–7. doi:10.1016/j.febslet.2008.07.033. PMID 18671972.
  20. ↑ Nagamine T, Nomada S, Onouchi T, Kameshita I, Sueyoshi N (Mar 2014). "Nuclear translocation of doublecortin-like protein kinase and phosphorylation of a transcription factor JDP2". Biochemical and Biophysical Research Communications. 446 (1): 73–8. doi:10.1016/j.bbrc.2014.02.075. PMID 24582561.
  21. ↑ 21.0 21.1 21.2 Huang YC, Saito S, Yokoyama KK (Oct 2010). "Histone chaperone Jun dimerization protein 2 (JDP2): role in cellular senescence and aging". The Kaohsiung Journal of Medical Sciences. 26 (10): 515–31. doi:10.1016/S1607-551X(10)70081-4. PMID 20950777.
  22. ↑ 22.0 22.1 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): 305–6. PMID 14510502.
  23. ↑ 23.0 23.1 23.2 23.3 23.4 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. 1819 (11–12): 1142–53. doi:10.1016/j.bbagrm.2012.09.005. PMC 3551276. PMID 22989952.
  24. ↑ Heideman MR, Wilting RH, Yanover E, Velds A, de Jong J, Kerkhoven RM, Jacobs H, Wessels LF, Dannenberg JH (Mar 2013). "Dosage-dependent tumor suppression by histone deacetylases 1 and 2 through regulation of c-Myc collaborating genes and p53 function". Blood. 121 (11): 2038–50. doi:10.1182/blood-2012-08-450916. PMC 3596963. PMID 23327920.
  25. ↑ 25.0 25.1 25.2 Jin C, Li H, Murata T, Sun K, Horikoshi M, Chiu R, Yokoyama KK (Jul 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): 4815–26. doi:10.1128/mcb.22.13.4815-4826.2002. PMC 133911. PMID 12052888.
  26. ↑ 26.0 26.1 Nakade K, Pan J, Yamasaki T, Murata T, Wasylyk B, Yokoyama KK (Apr 2009). "JDP2 (Jun Dimerization Protein 2)-deficient mouse embryonic fibroblasts are resistant to replicative senescence". The Journal of Biological Chemistry. 284 (16): 10808–17. doi:10.1074/jbc.M808333200. PMC 2667768. PMID 19233846.
  27. ↑ 27.0 27.1 27.2 Maruyama K, Fukasaka M, Vandenbon A, Saitoh T, Kawasaki T, Kondo T, Yokoyama KK, Kidoya H, Takakura N, Standley D, Takeuchi O, Akira S (Dec 2012). "The transcription factor Jdp2 controls bone homeostasis and antibacterial immunity by regulating osteoclast and neutrophil differentiation". Immunity. 37 (6): 1024–36. doi:10.1016/j.immuni.2012.08.022. PMID 23200825.
  28. ↑ Kehat I, Heinrich R, Ben-Izhak O, Miyazaki H, Gutkind JS, Aronheim A (Jun 2006). "Inhibition of basic leucine zipper transcription is a major mediator of atrial dilatation". Cardiovascular Research. 70 (3): 543–54. doi:10.1016/j.cardiores.2006.02.018. PMID 16631626.
  29. ↑ Kehat I, Hasin T, Aronheim A (Oct 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: 97–109. doi:10.1196/annals.1380.009. PMID 17132778.
  30. ↑ 30.0 30.1 Chérasse Y, Chaveroux C, Jousse C, Maurin AC, Carraro V, Parry L, Fafournoux P, Bruhat A (Apr 2008). "Role of the repressor JDP2 in the amino acid-regulated transcription of CHOP". FEBS Letters. 582 (10): 1537–41. doi:10.1016/j.febslet.2008.03.050. PMID 18396163.
  31. ↑ Weidenfeld-Baranboim K, Bitton-Worms K, Aronheim A (Jun 2008). "TRE-dependent transcription activation by JDP2-CHOP10 association". Nucleic Acids Research. 36 (11): 3608–19. doi:10.1093/nar/gkn268. PMC 2441799. PMID 18463134.
  32. ↑ Hill KK, Roemer SC, Jones DN, Churchill ME, Edwards DP (Sep 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): 24415–24. doi:10.1074/jbc.M109.003244. PMC 2782034. PMID 19553667.
  33. ↑ Wardell SE, Boonyaratanakornkit V, Adelman JS, Aronheim A, Edwards DP (Aug 2002). "Jun dimerization protein 2 functions as a progesterone receptor N-terminal domain coactivator". Molecular and Cellular Biology. 22 (15): 5451–66. doi:10.1128/mcb.22.15.5451-5466.2002. PMC 133955. PMID 12101239.
  34. ↑ Edwards DP, Wardell SE, Boonyaratanakornkit V (Dec 2002). "Progesterone receptor interacting coregulatory proteins and cross talk with cell signaling pathways". The Journal of Steroid Biochemistry and Molecular Biology. 83 (1–5): 173–86. doi:10.1016/s0960-0760(02)00265-0. PMID 12650714.
  35. ↑ Broder YC, Katz S, Aronheim A (Oct 1998). "The ras recruitment system, a novel approach to the study of protein-protein interactions". Current Biology. 8 (20): 1121–4. doi:10.1016/s0960-9822(98)70467-1. PMID 9778531.
  36. ↑ Nakade K, Pan J, Yoshiki A, Ugai H, Kimura M, Liu B, Li H, Obata Y, Iwama M, Itohara S, Murata T, Yokoyama KK (Aug 2007). "JDP2 suppresses adipocyte differentiation by regulating histone acetylation". Cell Death and Differentiation. 14 (8): 1398–405. doi:10.1038/sj.cdd.4402129. PMID 17464331.
  37. ↑ 37.0 37.1 37.2 37.3 Ostrovsky O, Bengal E, Aronheim A (Oct 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): 40043–54. doi:10.1074/jbc.M205494200. PMID 12171923.
  38. ↑ Kawaida R, Ohtsuka T, Okutsu J, Takahashi T, Kadono Y, Oda H, Hikita A, Nakamura K, Tanaka S, Furukawa H (Apr 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): 1029–35. doi:10.1084/jem.20021321. PMC 2193879. PMID 12707301.
  39. ↑ Yao C, Yao GQ, Sun BH, Zhang C, Tommasini SM, Insogna K (Mar 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): 6775–90. doi:10.1074/jbc.M113.499210. PMC 3945339. PMID 24394418.
  40. ↑ Ji H, Ehrlich LI, Seita J, Murakami P, Doi A, Lindau P, Lee H, Aryee MJ, Irizarry RA, Kim K, Rossi DJ, Inlay MA, Serwold T, Karsunky H, Ho L, Daley GQ, Weissman IL, Feinberg AP (Sep 2010). "Comprehensive methylome map of lineage commitment from haematopoietic progenitors". Nature. 467 (7313): 338–42. doi:10.1038/nature09367. PMC 2956609. PMID 20720541.
  41. ↑ 41.0 41.1 Heinrich R, Livne E, Ben-Izhak O, Aronheim A (Feb 2004). "The c-Jun dimerization protein 2 inhibits cell transformation and acts as a tumor suppressor gene". The Journal of Biological Chemistry. 279 (7): 5708–15. doi:10.1074/jbc.M307608200. PMID 14627710.
  42. ↑ 42.0 42.1 van der Weyden L, Rust AG, McIntyre RE, Robles-Espinoza CD, del Castillo Velasco-Herrera M, Strogantsev R, Ferguson-Smith AC, McCarthy S, Keane TM, Arends MJ, Adams DJ (Jan 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.
  43. ↑ Xu Y, Jin C, Liu Z, Pan J, Li H, Zhang Z, Bi S, Yokoyama KK (Aug 2014). "Cloning and characterization of the mouse JDP2 gene promoter reveal negative regulation by p53". Biochemical and Biophysical Research Communications. 450 (4): 1531–6. doi:10.1016/j.bbrc.2014.07.034. PMID 25026555.
  44. ↑ Lerdrup M, Holmberg C, Dietrich N, Shaulian E, Herdegen T, Jäättelä M, Kallunki T (Aug 2005). "Depletion of the AP-1 repressor JDP2 induces cell death similar to apoptosis". Biochimica et Biophysica Acta. 1745 (1): 29–37. doi:10.1016/j.bbamcr.2005.06.008. PMID 16026868.
  45. ↑ 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): 3012–24. doi:10.1128/MCB.21.9.3012-3024.2001. PMC 86930. PMID 11287607.
  46. ↑ Hill C, Würfel A, Heger J, Meyering B, Schlüter KD, Weber M, Ferdinandy P, Aronheim A, Schulz R, Euler G (Jul 2013). "Inhibition of AP-1 signaling by JDP2 overexpression protects cardiomyocytes against hypertrophy and apoptosis induction". Cardiovascular Research. 99 (1): 121–8. doi:10.1093/cvr/cvt094. PMID 23612584.
  47. ↑ Wang SW, Lee JK, Ku CC, Chiou SS, Steve Lin CL, Ho MF, Wu DC, Yokoyama KK (2011). "Jun dimerization protein 2 in oxygen restriction; control of senescence". Current Pharmaceutical Design. 17 (22): 2278–89. doi:10.2174/138161211797052394. PMID 21736542.
  48. ↑ 48.0 48.1 Tanigawa S, Lee CH, Lin CS, Ku CC, Hasegawa H, Qin S, Kawahara A, Korenori Y, Miyamori K, Noguchi M, Lee LH, Lin YC, Steve Lin CL, Nakamura Y, Jin C, Yamaguchi N, Eckner R, Hou DX, Yokoyama KK (14 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: e921. doi:10.1038/cddis.2013.448. PMC 3847324. PMID 24232097.
  49. ↑ Liu J, Han Q, Peng T, Peng M, Wei B, Li D, Wang X, Yu S, Yang J, Cao S, Huang K, Hutchins AP, Liu H, Kuang J, Zhou Z, Chen J, Wu H, Guo L, Chen Y, Chen Y, Li X, Wu H, Liao B, He W, Song H, Yao H, Pan G, Chen J, Pei D (Jul 2015). "The oncogene c-Jun impedes somatic cell reprogramming". Nature Cell Biology. 17 (7): 856–67. doi:10.1038/ncb3193. PMID 26098572.
  50. ↑ Hwang HC, Martins CP, Bronkhorst Y, Randel E, Berns A, Fero M, Clurman BE (Aug 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): 11293–8. doi:10.1073/pnas.162356099. PMC 123250. PMID 12151601.
  51. ↑ Rasmussen MH, Ballarín-González B, Liu J, Lassen LB, Füchtbauer A, Füchtbauer EM, Nielsen AL, Pedersen FS (Apr 2010). "Antisense transcription in gammaretroviruses as a mechanism of insertional activation of host genes". Journal of Virology. 84 (8): 3780–8. doi:10.1128/JVI.02088-09. PMC 2849499. PMID 20130045.
  52. ↑ Bitton-Worms K, Pikarsky E, Aronheim A (9 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.
  53. ↑ Järvinen AK, Autio R, Kilpinen S, Saarela M, Leivo I, Grénman R, Mäkitie AA, Monni O (Jun 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): 500–9. doi:10.1002/gcc.20551. PMID 18314910.
  54. ↑ 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): 136–40. PMID 20677166.
  55. ↑ Liu Z, Du R, Long J, Dong A, Fan J, Guo K, Xu Y (Oct 2012). "JDP2 inhibits the epithelial-to-mesenchymal transition in pancreatic cancer BxPC3 cells". Tumour Biology. 33 (5): 1527–34. doi:10.1007/s13277-012-0404-5. PMID 22535371.
  56. ↑ Maciejak A, Kiliszek M, Michalak M, Tulacz D, Opolski G, Matlak K, Dobrzycki S, Segiet A, Gora M, Burzynska B (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.
  57. ↑ Barkan B, Cox AD, Kloog Y (Feb 2013). "Ras inhibition boosts galectin-7 at the expense of galectin-1 to sensitize cells to apoptosis". Oncotarget. 4 (2): 256–68. doi:10.18632/oncotarget.844. PMC 3712571. PMID 23530091.
  58. ↑ Murata T, Noda C, Saito S, Kawashima D, Sugimoto A, Isomura H, Kanda T, Yokoyama KK, Tsurumi T (Jun 2011). "Involvement of Jun dimerization protein 2 (JDP2) in the maintenance of Epstein-Barr virus latency". The Journal of Biological Chemistry. 286 (25): 22007–16. doi:10.1074/jbc.M110.199836. PMC 3121345. PMID 21525011.

Further reading

  • Lerdrup M, Holmberg C, Dietrich N, Shaulian E, Herdegen T, Jäättelä M, Kallunki T (Aug 2005). "Depletion of the AP-1 repressor JDP2 induces cell death similar to apoptosis". Biochimica et Biophysica Acta. 1745 (1): 29–37. doi:10.1016/j.bbamcr.2005.06.008. PMID 16026868.

External links

Retrieved from "https://www.wikidoc.org/index.php?title=Jun_dimerization_protein&oldid=1521277"