DUSP5

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

{{Infobox_gene}}

Dual specificity protein phosphatase 5 is an enzyme that in humans is encoded by the DUSP5 gene.{{cite journal | vauthors = Martell KJ, Kwak S, Hakes DJ, Dixon JE, Trent JM | title = Chromosomal localization of four human VH1-like protein-tyrosine phosphatases | journal = Genomics | volume = 22 | issue = 2 | pages = 462–4 | date = Jul 1994 | pmid = 7806236 | doi = 10.1006/geno.1994.1411 | hdl = 2027.42/31442 | hdl-access = free }}{{cite web | title = Entrez Gene: DUSP5 dual specificity phosphatase 5| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1847}}

Function

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 product inactivates ERK1/2, is expressed in a variety of tissues with the highest levels in pancreas and brain, and is localized in the nucleus.

References

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Further reading

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  • {{cite journal | vauthors = Robertson NG, Khetarpal U, Gutiérrez-Espeleta GA, Bieber FR, Morton CC | title = Isolation of novel and known genes from a human fetal cochlear cDNA library using subtractive hybridization and differential screening | journal = Genomics | volume = 23 | issue = 1 | pages = 42–50 | date = Sep 1994 | pmid = 7829101 | doi = 10.1006/geno.1994.1457 }}
  • {{cite journal | vauthors = Kwak SP, Dixon JE | title = Multiple dual specificity protein tyrosine phosphatases are expressed and regulated differentially in liver cell lines | journal = The Journal of Biological Chemistry | volume = 270 | issue = 3 | pages = 1156–60 | date = Jan 1995 | pmid = 7836374 | doi = 10.1074/jbc.270.3.1156 | doi-access = free }}
  • {{cite journal | vauthors = Ishibashi T, Bottaro DP, Michieli P, Kelley CA, Aaronson SA | title = A novel dual specificity phosphatase induced by serum stimulation and heat shock | journal = The Journal of Biological Chemistry | volume = 269 | issue = 47 | pages = 29897–902 | date = Nov 1994 | doi = 10.1016/S0021-9258(18)43965-8 | pmid = 7961985 | doi-access = free }}
  • {{cite journal | vauthors = Ueda K, Arakawa H, Nakamura Y | title = Dual-specificity phosphatase 5 (DUSP5) as a direct transcriptional target of tumor suppressor p53 | journal = Oncogene | volume = 22 | issue = 36 | pages = 5586–91 | date = Aug 2003 | pmid = 12944906 | doi = 10.1038/sj.onc.1206845 | doi-access = free }}
  • {{cite journal | vauthors = Mandl M, Slack DN, Keyse SM | title = Specific inactivation and nuclear anchoring of extracellular signal-regulated kinase 2 by the inducible dual-specificity protein phosphatase DUSP5 | journal = Molecular and Cellular Biology | volume = 25 | issue = 5 | pages = 1830–45 | date = Mar 2005 | pmid = 15713638 | pmc = 549372 | doi = 10.1128/MCB.25.5.1830-1845.2005 }}
  • {{cite journal | vauthors = Jeong DG, Cho YH, Yoon TS, Kim JH, Ryu SE, Kim SJ | title = Crystal structure of the catalytic domain of human DUSP5, a dual specificity MAP kinase protein phosphatase | journal = Proteins | volume = 66 | issue = 1 | pages = 253–8 | date = Jan 2007 | pmid = 17078075 | doi = 10.1002/prot.21224 | s2cid = 30285092 | doi-access = free }}
  • {{cite journal | vauthors = Sarközi R, Miller B, Pollack V, Feifel E, Mayer G, Sorokin A, Schramek H | title = ERK1/2-driven and MKP-mediated inhibition of EGF-induced ERK5 signaling in human proximal tubular cells | journal = Journal of Cellular Physiology | volume = 211 | issue = 1 | pages = 88–100 | date = Apr 2007 | pmid = 17131384 | doi = 10.1002/jcp.20909 | s2cid = 39397816 }}

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