Jun dimerization protein
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| Location (UCSC) | Chr 14: 75.43 – 75.47 Mb | Chr 12: 85.65 – 85.69 Mb | |||||||
| PubMed search | [3] | [4] | |||||||
| View/Edit Human | View/Edit Mouse |
Jun dimerization protein 2 (JUNDM2) is a
JDP 2 was found by a Sos-recruitment system,[
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
Posttranscriptional and post translational modifications
Function
Phenotypes of gene knockout and transgenic mice
Gene
Dimer formation and interacting molecules
JDP2 functions as a transcription
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
Nuclear reprogramming
JDP2, which has been shown to regulate
Oncogene or tumor suppressor gene
JDP2 may act as a double-edge sword in
Cancer and disease markers
JDP2 shows the gene amplification of
JDP2 targets and JDP2-regulated genes
JDP2 is involved in the modulation of gene expression. For example, JDP2 regulates
Interactions
JDP2 (gene) has been shown to
Notes
Wikidata Q38797272 . |
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000140044 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000034271 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ PMID 9154808.
- ^ PMID 17545590.
- ^ "Entrez Gene: JDP2 jun dimerization protein 2".
- ^ S2CID 43837367.
- ^ PMID 12687017.
- ^ GeneCard for JDP2
- ^ a b Universal protein resource accession number Q8WYK2 at UniProt.
- ^ PMID 15913695.
- ^ PMID 19502497.
- PMID 19233874.
- ^ S2CID 21957070.
- ^ PMID 20802531.
- ^ PMID 24202329.
- S2CID 28550508.
- S2CID 43077117.
- ^ PMID 12225289.
- ^ PMID 18307971.
- S2CID 11422858.
- ^ S2CID 5226333.
- PMID 24582561.
- ^ PMID 20950777.
- ^ PMID 14510502.
- ^ PMID 22989952.
- PMID 23327920.
- ^ PMID 12052888.
- ^ PMID 19233846.
- ^ PMID 23200825.
- PMID 16631626.
- S2CID 19775029.
- ^ S2CID 8438516.
- PMID 18463134.
- PMID 19553667.
- PMID 12101239.
- S2CID 22258908.
- S2CID 16085672.
- PMID 17464331.
- ^ PMID 12171923.
- PMID 12707301.
- PMID 24394418.
- PMID 20720541.
- ^ PMID 14627710.
- ^ PMID 22370638.
- PMID 25026555.
- PMID 16026868.
- PMID 11287607.
- PMID 23612584.
- PMID 21736542.
- ^ PMID 24232097.
- S2CID 24437051.
- PMID 12151601.
- PMID 20130045.
- PMID 20214788.
- S2CID 9442226.
- S2CID 208044673.
- S2CID 15934564.
- PMID 25984239.)
{{cite journal}}: CS1 maint: DOI inactive as of April 2024 (link - PMID 29941549.
- PMID 23530091.
- PMID 21525011.
Further reading
- Lerdrup M, Holmberg C, Dietrich N, Shaulian E, Herdegen T, Jäättelä M, et al. (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. PMID 16026868.
External links
- JDP2 protein at the U.S. National Library of Medicine Medical Subject Headings (MeSH)