Entry - *608657 - JUN DIMERIZATION PROTEIN 2; JDP2 - OMIM
 
* 608657

JUN DIMERIZATION PROTEIN 2; JDP2


HGNC Approved Gene Symbol: JDP2

Cytogenetic location: 14q24.3   Genomic coordinates (GRCh38) : 14:75,426,943-75,474,107 (from NCBI)


TEXT

Cloning and Expression

Kawaida et al. (2003) stated that mouse Jdp2 has an N-terminal domain, a central basic region-leucine zipper domain, and a C-terminal domain.


Gene Function

Jin et al. (2002) found that mouse Jdp2 is an inhibitory subunit of the differentiation regulatory factor (DRF) complex. Jdp2 repressed retinoic acid-induced transcription of the Jun gene (165160) by recruiting a histone deacetylase-3 (HDAC3; 605166)-containing complex to the differentiation response element (DRE) of the Jun promoter.

Kawaida et al. (2003) found that overexpression of mouse Jdp2 activated the promoters of Trap (601895) and cathepsin K (601105) in a mouse hematopoietic progenitor cell line. Overexpression of Jdp2 also facilitated Rankl (602642)-mediated formation of Trap-positive multinuclear osteoclasts, and Jdp2 antisense oligonucleotides suppressed Rankl-induced osteoclast differentiation.

Heinrich et al. (2004) found that expression of JDP2 was reduced in several human cancers compared with matched normal tissues. Using several methods, they showed that human JDP2 has antitumorigenic properties. Heinrich et al. (2004) suggested that tumor suppression by JDP2 can be partially explained by the formation of inhibitory AP1 complexes via increased JUNB (165161), JUND (165162), and FRA2 (601575) expression and decreased JUN expression.

Using epitope tagging with coimmunoprecipitation analysis for confirmation, Kimura (2008) identified IRF2BP1 (615331) as a JDP2-binding protein. IRF2BP1 enhanced ubiquitination of JDP2, which required the IRF2BP1 RING finger domain. IRF2BP1 repressed ATF2 (123811)-mediated transcriptional activation in the absence of JDP2, as shown by luciferase analysis, independently of IRF2BP1 ubiquitin ligase activity. Coexpression analysis showed that the repressive effects of IRF2BP1 and JDP2 on ATF-dependent activation were additive. Protein pull-down assays showed that IRF2BP1 interacted with ATF2 directly.

Ji et al. (2010) examined 4.6 million CpG sites throughout the mouse genome for multipotent progenitors (MPPs), common lymphoid progenitors (CLPs), common myeloid progenitors (CMPs), granulocyte/macrophage progenitors (GMPs), and thymocyte progenitors. Many examples of genes and pathways not previously known to be involved in choice between lymphoid/myeloid differentiation were identified, such as Arl4c (604787) and Jdp2. Ji et al. (2010) concluded that their data provided a comprehensive map of the methylome during myeloid and lymphoid commitment from hematopoietic progenitors.


Mapping

Gross (2013) mapped the JDP2 gene to chromosome 14q24.3 based on an alignment of the JDP2 sequence (GenBank AB077880) with the genomic sequence.


REFERENCES

  1. Gross, M. B. Personal Communication. Baltimore, Md. 7/23/2013.

  2. Heinrich, R., Livne, E., Ben-Izhak, O., Aronheim, A. The c-Jun dimerization protein 2 inhibits cell transformation and acts as a tumor suppressor gene. J. Biol. Chem. 279: 5708-5715, 2004. [PubMed: 14627710, related citations] [Full Text]

  3. Ji, H., Ehrlich, L. I. R., Seita, J., Murakami, P., Doi, A., Lindau, P., Lee, H., Aryee, M. J., Irizarry, R. A., Kim, K., Rossi, D. J., Inlay, M. A., Serwold, T., Karsunky, H., Ho, L., Daley, G. Q., Weissman, I. L., Feinberg, A. P. Comprehensive methylome map of lineage commitment from haematopoietic progenitors. Nature 467: 338-342, 2010. [PubMed: 20720541, images, related citations] [Full Text]

  4. Jin, C., Li, H., Murata, T., Sun, K., Horikoshi, M., Chiu, R., Yokoyama, K. K. JDP2, a repressor of AP-1, recruits a histone deacetylase 3 complex to inhibit the retinoic acid-induced differentiation of F9 cells. Molec. Cell. Biol. 22: 4815-4826, 2002. [PubMed: 12052888, images, related citations] [Full Text]

  5. Kawaida, R., Ohtsuka, T., Okutsu, J., Takahashi, T., Kadono, Y., Oda, H., Hikita, A., Nakamura, K., Tanaka, S., Furukawa, H. Jun dimerization protein 2 (JDP2), a member of the AP-1 family of transcription factor, mediates osteoclast differentiation induced by RANKL. J. Exp. Med. 197: 1029-1035, 2003. [PubMed: 12707301, images, related citations] [Full Text]

  6. Kimura, M. IRF2-binding protein-1 is a JDP2 ubiquitin ligase and an inhibitor of ATF2-dependent transcription. FEBS Lett. 582: 2833-2837, 2008. [PubMed: 18671972, related citations] [Full Text]


Matthew B. Gross - updated : 7/23/2013
Paul J. Converse - updated : 7/23/2013
Ada Hamosh - updated : 9/29/2010
Creation Date:
Patricia A. Hartz : 5/14/2004
carol : 06/24/2016
mgross : 7/23/2013
mgross : 7/23/2013
alopez : 10/5/2010
alopez : 10/5/2010
terry : 9/29/2010
mgross : 5/14/2004
mgross : 5/14/2004

* 608657

JUN DIMERIZATION PROTEIN 2; JDP2


HGNC Approved Gene Symbol: JDP2

Cytogenetic location: 14q24.3   Genomic coordinates (GRCh38) : 14:75,426,943-75,474,107 (from NCBI)


TEXT

Cloning and Expression

Kawaida et al. (2003) stated that mouse Jdp2 has an N-terminal domain, a central basic region-leucine zipper domain, and a C-terminal domain.


Gene Function

Jin et al. (2002) found that mouse Jdp2 is an inhibitory subunit of the differentiation regulatory factor (DRF) complex. Jdp2 repressed retinoic acid-induced transcription of the Jun gene (165160) by recruiting a histone deacetylase-3 (HDAC3; 605166)-containing complex to the differentiation response element (DRE) of the Jun promoter.

Kawaida et al. (2003) found that overexpression of mouse Jdp2 activated the promoters of Trap (601895) and cathepsin K (601105) in a mouse hematopoietic progenitor cell line. Overexpression of Jdp2 also facilitated Rankl (602642)-mediated formation of Trap-positive multinuclear osteoclasts, and Jdp2 antisense oligonucleotides suppressed Rankl-induced osteoclast differentiation.

Heinrich et al. (2004) found that expression of JDP2 was reduced in several human cancers compared with matched normal tissues. Using several methods, they showed that human JDP2 has antitumorigenic properties. Heinrich et al. (2004) suggested that tumor suppression by JDP2 can be partially explained by the formation of inhibitory AP1 complexes via increased JUNB (165161), JUND (165162), and FRA2 (601575) expression and decreased JUN expression.

Using epitope tagging with coimmunoprecipitation analysis for confirmation, Kimura (2008) identified IRF2BP1 (615331) as a JDP2-binding protein. IRF2BP1 enhanced ubiquitination of JDP2, which required the IRF2BP1 RING finger domain. IRF2BP1 repressed ATF2 (123811)-mediated transcriptional activation in the absence of JDP2, as shown by luciferase analysis, independently of IRF2BP1 ubiquitin ligase activity. Coexpression analysis showed that the repressive effects of IRF2BP1 and JDP2 on ATF-dependent activation were additive. Protein pull-down assays showed that IRF2BP1 interacted with ATF2 directly.

Ji et al. (2010) examined 4.6 million CpG sites throughout the mouse genome for multipotent progenitors (MPPs), common lymphoid progenitors (CLPs), common myeloid progenitors (CMPs), granulocyte/macrophage progenitors (GMPs), and thymocyte progenitors. Many examples of genes and pathways not previously known to be involved in choice between lymphoid/myeloid differentiation were identified, such as Arl4c (604787) and Jdp2. Ji et al. (2010) concluded that their data provided a comprehensive map of the methylome during myeloid and lymphoid commitment from hematopoietic progenitors.


Mapping

Gross (2013) mapped the JDP2 gene to chromosome 14q24.3 based on an alignment of the JDP2 sequence (GenBank AB077880) with the genomic sequence.


REFERENCES

  1. Gross, M. B. Personal Communication. Baltimore, Md. 7/23/2013.

  2. Heinrich, R., Livne, E., Ben-Izhak, O., Aronheim, A. The c-Jun dimerization protein 2 inhibits cell transformation and acts as a tumor suppressor gene. J. Biol. Chem. 279: 5708-5715, 2004. [PubMed: 14627710] [Full Text: https://doi.org/10.1074/jbc.M307608200]

  3. Ji, H., Ehrlich, L. I. R., Seita, J., Murakami, P., Doi, A., Lindau, P., Lee, H., Aryee, M. J., Irizarry, R. A., Kim, K., Rossi, D. J., Inlay, M. A., Serwold, T., Karsunky, H., Ho, L., Daley, G. Q., Weissman, I. L., Feinberg, A. P. Comprehensive methylome map of lineage commitment from haematopoietic progenitors. Nature 467: 338-342, 2010. [PubMed: 20720541] [Full Text: https://doi.org/10.1038/nature09367]

  4. Jin, C., Li, H., Murata, T., Sun, K., Horikoshi, M., Chiu, R., Yokoyama, K. K. JDP2, a repressor of AP-1, recruits a histone deacetylase 3 complex to inhibit the retinoic acid-induced differentiation of F9 cells. Molec. Cell. Biol. 22: 4815-4826, 2002. [PubMed: 12052888] [Full Text: https://doi.org/10.1128/MCB.22.13.4815-4826.2002]

  5. Kawaida, R., Ohtsuka, T., Okutsu, J., Takahashi, T., Kadono, Y., Oda, H., Hikita, A., Nakamura, K., Tanaka, S., Furukawa, H. Jun dimerization protein 2 (JDP2), a member of the AP-1 family of transcription factor, mediates osteoclast differentiation induced by RANKL. J. Exp. Med. 197: 1029-1035, 2003. [PubMed: 12707301] [Full Text: https://doi.org/10.1084/jem.20021321]

  6. Kimura, M. IRF2-binding protein-1 is a JDP2 ubiquitin ligase and an inhibitor of ATF2-dependent transcription. FEBS Lett. 582: 2833-2837, 2008. [PubMed: 18671972] [Full Text: https://doi.org/10.1016/j.febslet.2008.07.033]


Contributors:
Matthew B. Gross - updated : 7/23/2013
Paul J. Converse - updated : 7/23/2013
Ada Hamosh - updated : 9/29/2010

Creation Date:
Patricia A. Hartz : 5/14/2004

Edit History:
carol : 06/24/2016
mgross : 7/23/2013
mgross : 7/23/2013
alopez : 10/5/2010
alopez : 10/5/2010
terry : 9/29/2010
mgross : 5/14/2004
mgross : 5/14/2004