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]
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]
- ^ 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.
- ^ a b c d 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.
- ^ Stewart M, Mackay N, Hanlon L, Blyth K, Scobie L, Cameron E, et al. (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.
- ^ "Entrez Gene: JDP2 jun dimerization protein 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.
- ^ 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.
- ^ GeneCard for JDP2
- ^ Universal protein resource accession number Q8WYK2 at UniProt.
- ^ a b 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.
- ^ 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.
- ^ 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.
- ^ 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.
- ^ 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.
- ^ 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.
- ^ 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.