Biology:JunD
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Short description: Protein-coding gene in the species Homo sapiens
 Generic protein structure example |
Transcription factor JunD is a protein that in humans is encoded by the JUND gene.[1][2]
Function
The protein encoded by this intronless gene is a member of the JUN family, and a functional component of the AP1 transcription factor complex. It has been proposed to protect cells from p53-dependent senescence and apoptosis. Alternate translation initiation site usage results in the production of different isoforms.[3]
ΔJunD
The dominant negative mutant variant of JunD, known as ΔJunD or Delta JunD, is a potent antagonist of the ΔFosB transcript, as well as other forms of AP-1-mediated transcriptional activity.[4][5][6] In the nucleus accumbens, ΔJunD directly opposes many of the neurological changes that occur in addiction (i.e., those induced by ΔFosB).[5][6] ΔFosB inhibitors (drugs that oppose its action) may be an effective treatment for addiction and addictive disorders.[7] Being an unnatural genetic variant, deltaJunD has not been observed in humans.
Interactions
JunD has been shown to interact with ATF3,[8] MEN1,[9] DNA damage-inducible transcript 3[10] and BRCA1.[11]
See also
- AP-1 (transcription factor)
References
- ↑ "Isolation of human cDNA clones of jun-related genes, jun-B and jun-D". Nucleic Acids Res. 18 (10): 3047–8. July 1990. doi:10.1093/nar/18.10.3047. PMID 2112242.
- ↑ "Structure and function of human jun-D". Oncogene 6 (4): 561–6. June 1991. PMID 1903194.
- ↑ "Entrez Gene: JUND jun D proto-oncogene". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3727.
- ↑ "Neural mechanisms of addiction: the role of reward-related learning and memory". Annu. Rev. Neurosci. 29: 565–98. 2006. doi:10.1146/annurev.neuro.29.051605.113009. PMID 16776597.
- ↑ 5.0 5.1 "Transcriptional and epigenetic mechanisms of addiction". Nat. Rev. Neurosci. 12 (11): 623–37. November 2011. doi:10.1038/nrn3111. PMID 21989194. "ΔFosB has been linked directly to several addiction-related behaviors ... Importantly, genetic or viral overexpression of ΔJunD, a dominant negative mutant of JunD which antagonizes ΔFosB- and other AP-1-mediated transcriptional activity, in the NAc or OFC blocks these key effects of drug exposure14,22–24. This indicates that ΔFosB is both necessary and sufficient for many of the changes wrought in the brain by chronic drug exposure. ΔFosB is also induced in D1-type NAc MSNs by chronic consumption of several natural rewards, including sucrose, high fat food, sex, wheel running, where it promotes that consumption14,26–30. This implicates ΔFosB in the regulation of natural rewards under normal conditions and perhaps during pathological addictive-like states.".
- ↑ 6.0 6.1 "ΔFosB in the nucleus accumbens is critical for reinforcing effects of sexual reward". Genes Brain Behav. 9 (7): 831–40. October 2010. doi:10.1111/j.1601-183X.2010.00621.x. PMID 20618447.
- ↑ "Chapter 15: Reinforcement and addictive disorders". Molecular Neuropharmacology: A Foundation for Clinical Neuroscience (2nd ed.). New York: McGraw-Hill Medical. 2009. pp. 384–385. ISBN 9780071481274.
- ↑ "Activating transcription factor-3 stimulates 3',5'-cyclic adenosine monophosphate-dependent gene expression". Mol. Endocrinol. 8 (1): 59–68. January 1994. doi:10.1210/mend.8.1.8152431. PMID 8152431.
- ↑ "Menin interacts with the AP1 transcription factor JunD and represses JunD-activated transcription". Cell 96 (1): 143–52. January 1999. doi:10.1016/S0092-8674(00)80967-8. PMID 9989505.
- ↑ "CHOP enhancement of gene transcription by interactions with Jun/Fos AP-1 complex proteins". Mol. Cell. Biol. 19 (11): 7589–99. November 1999. doi:10.1128/MCB.19.11.7589. PMID 10523647.
- ↑ "JunB potentiates function of BRCA1 activation domain 1 (AD1) through a coiled-coil-mediated interaction". Genes Dev. 16 (12): 1509–17. June 2002. doi:10.1101/gad.995502. PMID 12080089.
Further reading
- "Expression of c-jun, jun B and jun D proto-oncogenes in human peripheral-blood granulocytes". Biochem. J. 273(Pt 2) (2): 477–9. 1991. doi:10.1042/bj2730477. PMID 1899335.
- "In vitro association between the Jun protein family and the general transcription factors, TBP and TFIIB". Biochem. J. 305 (3): 967–74. 1995. doi:10.1042/bj3050967. PMID 7848298.
- "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1–2): 171–4. 1994. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
- "Activating transcription factor-3 stimulates 3',5'-cyclic adenosine monophosphate-dependent gene expression". Mol. Endocrinol. 8 (1): 59–68. 1994. doi:10.1210/mend.8.1.8152431. PMID 8152431.
- "Fluorescence in situ hybridization mapping of human chromosome 19: cytogenetic band location of 540 cosmids and 70 genes or DNA markers". Genomics 15 (1): 133–45. 1993. doi:10.1006/geno.1993.1021. PMID 8432525. https://zenodo.org/record/1229582.
- "B-ATF: a novel human bZIP protein that associates with members of the AP-1 transcription factor family". Oncogene 11 (11): 2255–65. 1995. PMID 8570175.
- "A new group of conserved coactivators that increase the specificity of AP-1 transcription factors". Nature 383 (6599): 453–7. 1996. doi:10.1038/383453a0. PMID 8837781. Bibcode: 1996Natur.383..453C.
- "c-Jun can recruit JNK to phosphorylate dimerization partners via specific docking interactions". Cell 87 (5): 929–39. 1996. doi:10.1016/S0092-8674(00)81999-6. PMID 8945519.
- "Isolation of an AP-1 repressor by a novel method for detecting protein-protein interactions". Mol. Cell. Biol. 17 (6): 3094–102. 1997. doi:10.1128/mcb.17.6.3094. PMID 9154808.
- "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–56. 1997. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
- "Decreased transcription factor junD in brains of patients with Down syndrome". Neurosci. Lett. 252 (3): 159–62. 1998. doi:10.1016/S0304-3940(98)00569-2. PMID 9739985.
- "Nrf2 and Nrf1 in association with Jun proteins regulate antioxidant response element-mediated expression and coordinated induction of genes encoding detoxifying enzymes". Oncogene 17 (24): 3145–56. 1998. doi:10.1038/sj.onc.1202237. PMID 9872330.
- "Menin interacts with the AP1 transcription factor JunD and represses JunD-activated transcription". Cell 96 (1): 143–52. 1999. doi:10.1016/S0092-8674(00)80967-8. PMID 9989505.
- "Smads bind directly to the Jun family of AP-1 transcription factors". Proc. Natl. Acad. Sci. U.S.A. 96 (9): 4844–9. 1999. doi:10.1073/pnas.96.9.4844. PMID 10220381. Bibcode: 1999PNAS...96.4844L.
- "Menin represses JunD-activated transcription by a histone deacetylase-dependent mechanism". Biochim. Biophys. Acta 1447 (1): 51–6. 1999. doi:10.1016/S0167-4781(99)00132-3. PMID 10500243.
- "CHOP enhancement of gene transcription by interactions with Jun/Fos AP-1 complex proteins". Mol. Cell. Biol. 19 (11): 7589–99. 1999. doi:10.1128/MCB.19.11.7589. PMID 10523647.
- "Interleukin-1beta induction of the chemokine RANTES promoter in the human astrocytoma line CH235 requires both constitutive and inducible transcription factors". J. Neuroimmunol. 105 (1): 78–90. 2000. doi:10.1016/S0165-5728(00)00195-8. PMID 10713367.
- "Regulation of AP1 (Jun/Fos) factor expression and activation in ovarian granulosa cells. Relation of JunD and Fra2 to terminal differentiation". J. Biol. Chem. 275 (43): 33718–28. 2000. doi:10.1074/jbc.M003555200. PMID 10934195.
External links
- JUND+protein,+human at the US National Library of Medicine Medical Subject Headings (MeSH)
- FactorBook JunD
- PDBe-KB provides an overview of all the structure information available in the PDB for Human Transcription factor jun-D
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
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