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JDP2  -  Jun dimerization protein 2

Homo sapiens

Synonyms: JUNDM2
 
 
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Disease relevance of JDP2

  • Using cell transformation assays in NIH3T3 cells and injection of prostate cancer cell lines overexpressing JDP2 into severe combined immuno-deficient (SCID) mice, we show for the first time the potential role of JDP2 in inhibition of cell transformation and tumor suppression [1].
  • On the other hand, JDP2 was shown to partially transform chicken embryo fibroblast and was identified in a screen for oncogenes able to collaborate with the loss of p27kip cyclin-dependent inhibitor to induce lymphomas [1].
  • Infection of mouse primary bone marrow cells with retroviruses expressing JDP2-facilitated sRANKL-mediated formation of TRAP-positive multinuclear osteoclasts [2].
  • PURPOSE: To identify the genotype of 18S ribosomal RNA gene (18S rDNA, Rns) of the Acanthamoeba strains isolated from patients with keratitis in northern China. METHODS: The genus-specific primers JDP1 and JDP2 were used for the amplification of the amplimer ASA.S1 [3].
 

High impact information on JDP2

  • Importantly, antisense oligonucleotide to JDP2 strongly suppressed sRANKL-induced osteoclast formation of RAW264.7 cells [2].
  • Our findings suggest that JDP2 may play an important role in the RANK-mediated signal transduction system, especially in osteoclast differentiation [2].
  • JDP-2 was first defined as a c-Jun interacting protein that functions as an AP-1 repressor [4].
  • JDP-2 has preferential activity on PR among the nuclear receptors tested and is expressed in progesterone target cells and tissues, suggesting that it has a physiological role in PR function [4].
  • The c-Jun dimerization protein, JDP2, is a member of the AP-1 (activating protein-1) family of the basic leucine zipper transcription factors [1].
 

Biological context of JDP2

  • JDP2 can bind 12-O-tetradecanoylphorbol-13-acetate (TPA)-responsive element and cAMP-responsive element DNA response elements, resulting in the inhibition of transcription [1].
  • Although the role of AP-1 in cell proliferation and malignant transformation is well established, the role of JDP2 in this process is of subject to debate [1].
  • Regulation of histone acetylation and nucleosome assembly by transcription factor JDP2 [5].
  • Depletion of the AP-1 repressor JDP2 induces cell death similar to apoptosis [6].
  • The first interaction (detailed here) is between JDP2, a member of the basic leucine zipper (bZIP) family, and C/EBPgamma, a member of the CCAAT/enhancer-binding protein (C/EBP) family [7].
 

Anatomical context of JDP2

 

Associations of JDP2 with chemical compounds

 

Physical interactions of JDP2

  • These results suggest that HDAC3/JDP2 and p300/ATF-2 complex play a critical role in controlling the differentiation of F9 cells, in response to RA [10].
 

Other interactions of JDP2

  • JDP-2, initially defined as a repressor of jun and other bZIP transcription factors, also functions as a potent PR selective coactivator [11].
  • Histone modification activities of JDP2 associated with retinoic acid-induced differentiation of F9 cells [10].
 

Analytical, diagnostic and therapeutic context of JDP2

  • Circular dichroism spectroscopy experiments showed that JDP-2 interaction caused a significant increase in overall helical content of a two-domain PR polypeptide containing the N-terminal domain and DBD and that the change in structure resides primarily in the N-terminal domain [12].

References

  1. The c-Jun dimerization protein 2 inhibits cell transformation and acts as a tumor suppressor gene. Heinrich, R., Livne, E., Ben-Izhak, O., Aronheim, A. J. Biol. Chem. (2004) [Pubmed]
  2. Jun dimerization protein 2 (JDP2), a member of the AP-1 family of transcription factor, mediates osteoclast differentiation induced by RANKL. Kawaida, R., Ohtsuka, T., Okutsu, J., Takahashi, T., Kadono, Y., Oda, H., Hikita, A., Nakamura, K., Tanaka, S., Furukawa, H. J. Exp. Med. (2003) [Pubmed]
  3. Identification of 18S ribosomal DNA genotype of Acanthamoeba from patients with keratitis in North China. Zhang, Y., Sun, X., Wang, Z., Li, R., Luo, S., Jin, X., Deng, S., Chen, W. Invest. Ophthalmol. Vis. Sci. (2004) [Pubmed]
  4. Jun dimerization protein 2 functions as a progesterone receptor N-terminal domain coactivator. Wardell, S.E., Boonyaratanakornkit, V., Adelman, J.S., Aronheim, A., Edwards, D.P. Mol. Cell. Biol. (2002) [Pubmed]
  5. Regulation of histone acetylation and nucleosome assembly by transcription factor JDP2. 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, K.K. Nat. Struct. Mol. Biol. (2006) [Pubmed]
  6. Depletion of the AP-1 repressor JDP2 induces cell death similar to apoptosis. Lerdrup, M., Holmberg, C., Dietrich, N., Shaulian, E., Herdegen, T., Jäättelä, M., Kallunki, T. Biochim. Biophys. Acta (2005) [Pubmed]
  7. The ras recruitment system, a novel approach to the study of protein-protein interactions. Broder, Y.C., Katz, S., Aronheim, A. Curr. Biol. (1998) [Pubmed]
  8. Inhibition of basic leucine zipper transcription is a major mediator of atrial dilatation. Kehat, I., Heinrich, R., Ben-Izhak, O., Miyazaki, H., Gutkind, J.S., Aronheim, A. Cardiovasc. Res. (2006) [Pubmed]
  9. The AP-1 repressor, JDP2, is a bona fide substrate for the c-Jun N-terminal kinase. Katz, S., Heinrich, R., Aronheim, A. FEBS Lett. (2001) [Pubmed]
  10. Histone modification activities of JDP2 associated with retinoic acid-induced differentiation of F9 cells. Pan, J., Jin, C., Murata, T., Yokoyama, K.K. Nucleic acids symposium series (2004) (2004) [Pubmed]
  11. Progesterone receptor interacting coregulatory proteins and cross talk with cell signaling pathways. Edwards, D.P., Wardell, S.E., Boonyaratanakornkit, V. J. Steroid Biochem. Mol. Biol. (2002) [Pubmed]
  12. Regulation of the amino-terminal transcription activation domain of progesterone receptor by a cofactor-induced protein folding mechanism. Wardell, S.E., Kwok, S.C., Sherman, L., Hodges, R.S., Edwards, D.P. Mol. Cell. Biol. (2005) [Pubmed]
 
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