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JunD

From Wikipedia, the free encyclopedia

Protein-coding gene in the species Homo sapiens
For the military districts under the early Caliphates, see Jund.

JUND
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

3U86

Identifiers
AliasesJUND, AP-1, JunD, JunD proto-oncogene, AP-1 transcription factor subunit
External IDsOMIM: 165162; MGI: 96648; HomoloGene: 3910; GeneCards: JUND; OMA:JUND - orthologs
Gene location (Human)
Chr.Chromosome 19 (human)[1]
Band19p13.11Start18,279,694 bp[1]
End18,281,622 bp[1]
Gene location (Mouse)
Chr.Chromosome 8 (mouse)[2]
Band8 B3.3|8 34.15 cMStart71,151,599 bp[2]
End71,153,265 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • cardia

  • vena cava

  • nipple

  • paraflocculus of cerebellum

  • pylorus

  • renal medulla

  • lactiferous duct

  • trachea

  • saphenous vein

  • Brodmann area 10
Top expressed in
  • granulocyte

  • adrenal gland

  • bone marrow

  • islet of Langerhans

  • ileum

  • ganglionic eminence

  • cerebellar cortex

  • primary visual cortex

  • striatum of neuraxis

  • urinary bladder
More reference expression data
BioGPS




More reference expression data
Gene ontology
Molecular function
Cellular component
Biological process
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

3727

16478

Ensembl

ENSG00000130522

ENSMUSG00000071076

UniProt

P17535

P15066

RefSeq (mRNA)

NM_005354
NM_001286968

NM_001286944
NM_010592

RefSeq (protein)

NP_001273897
NP_005345

NP_001273873
NP_034722

Location (UCSC)Chr 19: 18.28 - 18.28 MbChr 8: 71.15 - 71.15 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Transcription factor JunD is a protein that in humans is encoded by the JUND gene.[5][6]

Function

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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.[7]

DJunD

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The dominant negative mutant variant of JunD, known as DJunD or Delta JunD, is a potent antagonist of the DFosB transcript, as well as other forms of AP-1-mediated transcriptional activity.[8][9][10] In the nucleus accumbens, DJunD directly opposes many of the neurological changes that occur in addiction (i.e., those induced by DFosB).[9][10] DFosB inhibitors (drugs that oppose its action) may be an effective treatment for addiction and addictive disorders.[11] Being an unnatural genetic variant, DJunD has not been observed in humans.

Interactions

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JunD has been shown to interact with ATF3,[12] MEN1,[13] DNA damage-inducible transcript 3[14] and BRCA1.[15]

See also

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References

[edit]
  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000130522 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000071076 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Nomura N, Ide M, Sasamoto S, Matsui M, Date T, Ishizaki R (July 1990). "Isolation of human cDNA clones of jun-related genes, jun-B and jun-D". Nucleic Acids Res. 18 (10): 3047-8. doi:10.1093/nar/18.10.3047. PMC 330838. PMID 2112242.
  6. ^ Berger I, Shaul Y (June 1991). "Structure and function of human jun-D". Oncogene. 6 (4): 561-6. PMID 1903194.
  7. ^ "Entrez Gene: JUND jun D proto-oncogene".
  8. ^ Hyman SE, Malenka RC, Nestler EJ (2006). "Neural mechanisms of addiction: the role of reward-related learning and memory". Annu. Rev. Neurosci. 29: 565-98. doi:10.1146/annurev.neuro.29.051605.113009. PMID 16776597.
  9. ^ a b Robison AJ, Nestler EJ (November 2011). "Transcriptional and epigenetic mechanisms of addiction". Nat. Rev. Neurosci. 12 (11): 623-37. doi:10.1038/nrn3111. PMC 3272277. PMID 21989194. DFosB has been linked directly to several addiction-related behaviors ... Importantly, genetic or viral overexpression of DJunD, a dominant negative mutant of JunD which antagonizes DFosB- and other AP-1-mediated transcriptional activity, in the NAc or OFC blocks these key effects of drug exposure14,22-24. This indicates that DFosB is both necessary and sufficient for many of the changes wrought in the brain by chronic drug exposure. DFosB 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 DFosB in the regulation of natural rewards under normal conditions and perhaps during pathological addictive-like states.
  10. ^ a b Pitchers KK, Frohmader KS, Vialou V, Mouzon E, Nestler EJ, Lehman MN, Coolen LM (October 2010). "DFosB in the nucleus accumbens is critical for reinforcing effects of sexual reward". Genes Brain Behav. 9 (7): 831-40. doi:10.1111/j.1601-183X.2010.00621.x. PMC 2970635. PMID 20618447.
  11. ^ Malenka RC, Nestler EJ, Hyman SE (2009). "Chapter 15: Reinforcement and addictive disorders". In Sydor A, Brown RY (eds.). Molecular Neuropharmacology: A Foundation for Clinical Neuroscience (2nd ed.). New York: McGraw-Hill Medical. pp. 384-385. ISBN 9780071481274.
  12. ^ Chu HM, Tan Y, Kobierski LA, Balsam LB, Comb MJ (January 1994). "Activating transcription factor-3 stimulates 3',5'-cyclic adenosine monophosphate-dependent gene expression". Mol. Endocrinol. 8 (1): 59-68. doi:10.1210/mend.8.1.8152431. PMID 8152431.
  13. ^ Agarwal SK, Guru SC, Heppner C, Erdos MR, Collins RM, Park SY, Saggar S, Chandrasekharappa SC, Collins FS, Spiegel AM, Marx SJ, Burns AL (January 1999). "Menin interacts with the AP1 transcription factor JunD and represses JunD-activated transcription". Cell. 96 (1): 143-52. doi:10.1016/S0092-8674(00)80967-8. PMID 9989505. S2CID 18116746.
  14. ^ Ubeda M, Vallejo M, Habener JF (November 1999). "CHOP enhancement of gene transcription by interactions with Jun/Fos AP-1 complex proteins". Mol. Cell. Biol. 19 (11): 7589-99. doi:10.1128/MCB.19.11.7589. PMC 84780. PMID 10523647.
  15. ^ Hu YF, Li R (June 2002). "JunB potentiates function of BRCA1 activation domain 1 (AD1) through a coiled-coil-mediated interaction". Genes Dev. 16 (12): 1509-17. doi:10.1101/gad.995502. PMC 186344. PMID 12080089.

Further reading

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This article incorporates text from the United States National Library of Medicine, which is in the public domain.


(1) Basic domains
(1.1) Basic leucine zipper (bZIP)
(1.2) Basic helix-loop-helix (bHLH)
Group A
Group B
Group C
bHLH-PAS
Group D
Group E
Group F
bHLH-COE
(1.3) bHLH-ZIP
(1.4) NF-1
(1.5) RF-X
(1.6) Basic helix-span-helix (bHSH)
(2) Zinc finger DNA-binding domains
(2.1) Nuclear receptor (Cys4)
subfamily 1
subfamily 2
subfamily 3
subfamily 4
subfamily 5
subfamily 6
subfamily 0
(2.2) Other Cys4
(2.3) Cys2His2
(2.4) Cys6
(2.5) Alternating composition
(2.6) WRKY
(3) Helix-turn-helix domains
(3.1) Homeodomain
Antennapedia
ANTP class
protoHOX
Hox-like
metaHOX
NK-like
other
(3.2) Paired box
(3.3) Fork head / winged helix
(3.4) Heat shock factors
(3.5) Tryptophan clusters
(3.6) TEA domain
  • transcriptional enhancer factor
(4) b-Scaffold factors with minor groove contacts
(4.1) Rel homology region
(4.2) STAT
(4.3) p53-like
(4.4) MADS box
(4.6) TATA-binding proteins
(4.7) High-mobility group
(4.9) Grainyhead
(4.10) Cold-shock domain
(4.11) Runt
(0) Other transcription factors
(0.2) HMGI(Y)
(0.3) Pocket domain
(0.5) AP-2/EREBP-related factors
(0.6) Miscellaneous