DUSP3

{{Short description|Protein-coding gene in the species Homo sapiens}}

{{Infobox_gene}}

Dual specificity protein phosphatase 3 is an enzyme that in humans is encoded by the DUSP3 gene.{{cite journal | vauthors = Folander K, Douglass J, Swanson R | title = Confirmation of the assignment of the gene encoding Kv1.3, a voltage-gated potassium channel (KCNA3) to the proximal short arm of human chromosome 1 | journal = Genomics | volume = 23 | issue = 1 | pages = 295–6 |date=Feb 1995 | pmid = 7829094 | doi = 10.1006/geno.1994.1500 }}{{cite web | title = Entrez Gene: DUSP3 dual specificity phosphatase 3 (vaccinia virus phosphatase VH1-related)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1845}}

The protein encoded by this gene is a member of the dual specificity protein phosphatase subfamily. These phosphatases inactivate their target kinases by dephosphorylating both the phosphoserine/threonine and phosphotyrosine residues. They negatively regulate members of the mitogen-activated protein (MAP) kinase superfamily (MAPK/ERK, SAPK/JNK, p38), which are associated with cellular proliferation and differentiation. Different members of the family of dual specificity phosphatases show distinct substrate specificities for various MAP kinases, different tissue distribution and subcellular localization, and different modes of inducibility of their expression by extracellular stimuli. This gene maps in a region that contains the BRCA1 locus which confers susceptibility to breast and ovarian cancer. Although DUSP3 is expressed in both breast and ovarian tissues, mutation screening in breast cancer pedigrees and in sporadic tumors was negative, leading to the conclusion that this gene is not BRCA1.

Interactions

DUSP3 has been shown to interact with MAPK3{{cite journal |last=Todd |first=J L |author2=Tanner K G |author3=Denu J M |date=May 1999 |title=Extracellular regulated kinases (ERK) 1 and ERK2 are authentic substrates for the dual-specificity protein-tyrosine phosphatase VHR. A novel role in down-regulating the ERK pathway |journal=J. Biol. Chem. |volume=274 |issue=19 |pages=13271–80 |location = UNITED STATES| issn = 0021-9258| pmid = 10224087 |doi=10.1074/jbc.274.19.13271 |doi-access=free }} and MAPK1.

References

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Further reading

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  • {{cite journal | vauthors=Ishibashi T, Bottaro DP, Chan A |title=Expression cloning of a human dual-specificity phosphatase |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 24 |pages= 12170–4 |year= 1993 |pmid= 1281549 |doi=10.1073/pnas.89.24.12170 | pmc=50720 |display-authors=etal|bibcode=1992PNAS...8912170I|doi-access=free }}
  • {{cite journal |vauthors=Kamb A, Futreal PA, Rosenthal J |title=Localization of the VHR phosphatase gene and its analysis as a candidate for BRCA1 |journal=Genomics |volume=23 |issue=1 |pages=163–7 |year=1995 |pmid=7829067 |doi=10.1006/geno.1994.1473 |display-authors=etal |url=https://zenodo.org/record/1229638 }}
  • {{cite journal | vauthors=Jones KA, Black DM, Brown MA |title=The detailed characterisation of a 400 kb cosmid walk in the BRCA1 region: identification and localisation of 10 genes including a dual-specificity phosphatase |journal=Hum. Mol. Genet. |volume=3 |issue= 11 |pages= 1927–34 |year= 1995 |pmid= 7874108 |doi=10.1093/hmg/3.11.1927 |display-authors=etal}}
  • {{cite journal | vauthors=Yuvaniyama J, Denu JM, Dixon JE, Saper MA |title=Crystal structure of the dual specificity protein phosphatase VHR |journal=Science |volume=272 |issue= 5266 |pages= 1328–31 |year= 1996 |pmid= 8650541 |doi=10.1126/science.272.5266.1328 |bibcode=1996Sci...272.1328Y |s2cid=33816598 }}
  • {{cite journal | vauthors=Todd JL, Tanner KG, Denu JM |title=Extracellular regulated kinases (ERK) 1 and ERK2 are authentic substrates for the dual-specificity protein-tyrosine phosphatase VHR. A novel role in down-regulating the ERK pathway |journal=J. Biol. Chem. |volume=274 |issue= 19 |pages= 13271–80 |year= 1999 |pmid= 10224087 |doi=10.1074/jbc.274.19.13271 |doi-access=free }}
  • {{cite journal | vauthors=Alonso A, Saxena M, Williams S, Mustelin T |title=Inhibitory role for dual specificity phosphatase VHR in T cell antigen receptor and CD28-induced Erk and Jnk activation |journal=J. Biol. Chem. |volume=276 |issue= 7 |pages= 4766–71 |year= 2001 |pmid= 11085983 |doi= 10.1074/jbc.M006497200 |doi-access= free }}
  • {{cite journal | vauthors=Najarro P, Traktman P, Lewis JA |title=Vaccinia virus blocks gamma interferon signal transduction: viral VH1 phosphatase reverses Stat1 activation |journal=J. Virol. |volume=75 |issue= 7 |pages= 3185–96 |year= 2001 |pmid= 11238845 |doi= 10.1128/JVI.75.7.3185-3196.2001 | pmc=114112 }}
  • {{cite journal | vauthors=Alonso A, Rahmouni S, Williams S |title=Tyrosine phosphorylation of VHR phosphatase by ZAP-70 |journal=Nat. Immunol. |volume=4 |issue= 1 |pages= 44–8 |year= 2003 |pmid= 12447358 |doi= 10.1038/ni856 |s2cid=10205773 |display-authors=etal|doi-access=free }}
  • {{cite journal | vauthors=Strausberg RL, Feingold EA, Grouse LH |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 |display-authors=etal|bibcode=2002PNAS...9916899M |doi-access=free }}
  • {{cite journal |vauthors=Kim HS, Song MC, Kwak IH |title=Constitutive induction of p-Erk1/2 accompanied by reduced activities of protein phosphatases 1 and 2A and MKP3 due to reactive oxygen species during cellular senescence |journal=J. Biol. Chem. |volume=278 |issue=39 |pages=37497–510 |year=2003 |pmid=12840032 |doi=10.1074/jbc.M211739200 |s2cid=7806506 |display-authors=etal |doi-access=free }}
  • {{cite journal | vauthors=Ota T, Suzuki Y, Nishikawa T |title=Complete sequencing and characterization of 21,243 full-length human cDNAs |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 |display-authors=etal|doi-access=free }}
  • {{cite journal | vauthors=Gerhard DS, Wagner L, Feingold EA |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 |display-authors=etal}}
  • {{cite journal | vauthors=Rual JF, Venkatesan K, Hao T |title=Towards a proteome-scale map of the human protein-protein interaction network |journal=Nature |volume=437 |issue= 7062 |pages= 1173–8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209 |display-authors=etal|bibcode=2005Natur.437.1173R |s2cid=4427026 }}
  • {{cite journal | vauthors=Rahmouni S, Cerignoli F, Alonso A |title=Loss of the VHR dual-specific phosphatase causes cell-cycle arrest and senescence |journal=Nat. Cell Biol. |volume=8 |issue= 5 |pages= 524–31 |year= 2006 |pmid= 16604064 |doi= 10.1038/ncb1398 |s2cid=20976640 |display-authors=etal}}
  • {{cite journal | vauthors=Hao L, ElShamy WM |title=BRCA1-IRIS activates cyclin D1 expression in breast cancer cells by downregulating the JNK phosphatase DUSP3/VHR |journal=Int. J. Cancer |volume=121 |issue= 1 |pages= 39–46 |year= 2007 |pmid= 17278098 |doi= 10.1002/ijc.22597 |s2cid=24555741 |doi-access=free }}
  • {{cite journal | vauthors=Hoyt R, Zhu W, Cerignoli F |title=Cutting edge: selective tyrosine dephosphorylation of interferon-activated nuclear STAT5 by the VHR phosphatase |journal=J. Immunol. |volume=179 |issue= 6 |pages= 3402–6 |year= 2007 |pmid= 17785772 |doi= 10.4049/jimmunol.179.6.3402| pmc=2770724 |display-authors=etal}}

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{{PDB Gallery|geneid=1845}}

{{Protein tyrosine phosphatases}}

Category:Genes mutated in mice

Category:EC 3.1.3