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DUSP6

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(Redirected from MKP3)
DUSP6
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesDUSP6, HH19, MKP3, PYST1, dual specificity phosphatase 6
External IDsOMIM: 602748; MGI: 1914853; HomoloGene: 55621; GeneCards: DUSP6; OMA:DUSP6 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_022652
NM_001946

NM_026268

RefSeq (protein)

NP_001937
NP_073143

NP_080544

Location (UCSC)Chr 12: 89.35 – 89.35 MbChr 10: 99.1 – 99.1 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Dual specificity phosphatase 6 (DUSP6) is an enzyme that in humans is encoded by the DUSP6 gene.[5][6][7]

Function

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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 ERK2, is expressed in a variety of tissues with the highest levels in heart and pancreas and, unlike most other members of this family, is localized in the cytoplasm. Two transcript variants encoding different isoforms have been found for this gene.[5] Upregulation of MKP-3 has been shown to alleviate chronic postoperative pain.[8][9]

Interactions

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DUSP6 has been shown to interact with MAPK3.[10]

References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000139318Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000019960Ensembl, 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. ^ a b "Entrez Gene: DUSP6 dual specificity phosphatase 6".
  6. ^ Muda M, Boschert U, Dickinson R, Martinou JC, Martinou I, Camps M, Schlegel W, Arkinstall S (February 1996). "MKP-3, a novel cytosolic protein-tyrosine phosphatase that exemplifies a new class of mitogen-activated protein kinase phosphatase". The Journal of Biological Chemistry. 271 (8): 4319–26. doi:10.1074/jbc.271.8.4319. PMID 8626780.
  7. ^ Smith A, Price C, Cullen M, Muda M, King A, Ozanne B, Arkinstall S, Ashworth A (June 1997). "Chromosomal localization of three human dual specificity phosphatase genes (DUSP4, DUSP6, and DUSP7)". Genomics. 42 (3): 524–7. doi:10.1006/geno.1997.4756. PMID 9205128.
  8. ^ Saha M, Skopelja S, Martinez E, Alvarez DL, Liponis BS, Romero-Sandoval EA (October 2013). "Spinal mitogen-activated protein kinase phosphatase-3 (MKP-3) is necessary for the normal resolution of mechanical allodynia in a mouse model of acute postoperative pain". The Journal of Neuroscience. 33 (43): 17182–7. doi:10.1523/JNEUROSCI.5605-12.2013. PMC 6618446. PMID 24155322.
  9. ^ Skopelja-Gardner S, Saha M, Alvarado-Vazquez PA, Liponis BS, Martinez E, Romero-Sandoval EA (2017-03-28). "Mitogen-activated protein kinase phosphatase-3 (MKP-3) in the surgical wound is necessary for the resolution of postoperative pain in mice". Journal of Pain Research. 10: 763–774. doi:10.2147/jpr.s129826. PMC 5378457. PMID 28405172.
  10. ^ Muda M, Theodosiou A, Gillieron C, Smith A, Chabert C, Camps M, Boschert U, Rodrigues N, Davies K, Ashworth A, Arkinstall S (April 1998). "The mitogen-activated protein kinase phosphatase-3 N-terminal noncatalytic region is responsible for tight substrate binding and enzymatic specificity". The Journal of Biological Chemistry. 273 (15): 9323–9. doi:10.1074/jbc.273.15.9323. PMID 9535927.

Further reading

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  • Overview of all the structural information available in the PDB for UniProt: Q16828 (Dual specificity protein phosphatase 6) at the PDBe-KB.