DUSP1

From Wikipedia, the free encyclopedia

Dual specificity phosphatase 1

Identifiers

DUSP1; CL100; HVH1; MKP-1; PTPN10

External IDs

OMIM: 600714 MGI: 105120 HomoloGene: 3254

Gene ontology
Molecular Function:	• non-membrane spanning protein tyrosine phosphatase activity • protein binding • hydrolase activity • MAP kinase tyrosine/serine/threonine phosphatase activity
Biological Process:	• protein amino acid dephosphorylation • response to oxidative stress • cell cycle

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_004417 (mRNA)
NP_004408 (protein)

NM_013642 (mRNA)
NP_038670 (protein)

Location

Chr 5: 172.13 - 172.13 Mb

Chr 17: 26.23 - 26.24 Mb

Pubmed search

[1]

[2]

Dual specificity phosphatase 1, also known as DUSP1, is a human gene.

The expression of DUSP1 gene is induced in human skin fibroblasts by oxidative/heat stress and growth factors. It specifies a protein with structural features similar to members of the non-receptor-type protein-tyrosine phosphatase family, and which has significant amino-acid sequence similarity to a Tyr/Ser-protein phosphatase encoded by the late gene H1 of vaccinia virus. The bacterially expressed and purified DUSP1 protein has intrinsic phosphatase activity, and specifically inactivates mitogen-activated protein (MAP) kinase in vitro by the concomitant dephosphorylation of both its phosphothreonine and phosphotyrosine residues. Furthermore, it suppresses the activation of MAP kinase by oncogenic ras in extracts of Xenopus oocytes. Thus, DUSP1 may play an important role in the human cellular response to environmental stress as well as in the negative regulation of cellular proliferation.^[1]

[edit] References

^ Entrez Gene: DUSP1 dual specificity phosphatase 1.

[edit] Further reading

Martell KJ, Angelotti T, Ullrich A (1998). "The "VH1-like" dual-specificity protein tyrosine phosphatases.". Mol. Cells 8 (1): 2–11. PMID 9571625.
Keyse SM (1998). "Protein phosphatases and the regulation of MAP kinase activity.". Semin. Cell Dev. Biol. 9 (2): 143–52. doi:10.1006/scdb.1997.0219. PMID 9599409.
Abraham SM, Clark AR (2007). "Dual-specificity phosphatase 1: a critical regulator of innate immune responses.". Biochem. Soc. Trans. 34 (Pt 6): 1018–23. doi:10.1042/BST0341018. PMID 17073741.
Keyse SM, Emslie EA (1992). "Oxidative stress and heat shock induce a human gene encoding a protein-tyrosine phosphatase.". Nature 359 (6396): 644–7. doi:10.1038/359644a0. PMID 1406996.
Raingeaud J, Gupta S, Rogers JS, et al. (1995). "Pro-inflammatory cytokines and environmental stress cause p38 mitogen-activated protein kinase activation by dual phosphorylation on tyrosine and threonine.". J. Biol. Chem. 270 (13): 7420–6. PMID 7535770.
Martell KJ, Kwak S, Hakes DJ, et al. (1995). "Chromosomal localization of four human VH1-like protein-tyrosine phosphatases.". Genomics 22 (2): 462–4. doi:10.1006/geno.1994.1411. PMID 7806236.
Kwak SP, Hakes DJ, Martell KJ, Dixon JE (1994). "Isolation and characterization of a human dual specificity protein-tyrosine phosphatase gene.". J. Biol. Chem. 269 (5): 3596–604. PMID 8106404.
Emslie EA, Jones TA, Sheer D, Keyse SM (1994). "The CL100 gene, which encodes a dual specificity (Tyr/Thr) MAP kinase phosphatase, is highly conserved and maps to human chromosome 5q34.". Hum. Genet. 93 (5): 513–6. PMID 8168826.
Sun H, Charles CH, Lau LF, Tonks NK (1993). "MKP-1 (3CH134), an immediate early gene product, is a dual specificity phosphatase that dephosphorylates MAP kinase in vivo.". Cell 75 (3): 487–93. PMID 8221888.
Charles CH, Sun H, Lau LF, Tonks NK (1993). "The growth factor-inducible immediate-early gene 3CH134 encodes a protein-tyrosine-phosphatase.". Proc. Natl. Acad. Sci. U.S.A. 90 (11): 5292–6. PMID 8389479.
Alessi DR, Smythe C, Keyse SM (1993). "The human CL100 gene encodes a Tyr/Thr-protein phosphatase which potently and specifically inactivates MAP kinase and suppresses its activation by oncogenic ras in Xenopus oocyte extracts.". Oncogene 8 (7): 2015–20. PMID 8390041.
Brondello JM, Pouysségur J, McKenzie FR (2000). "Reduced MAP kinase phosphatase-1 degradation after p42/p44MAPK-dependent phosphorylation.". Science 286 (5449): 2514–7. PMID 10617468.
Hutter D, Chen P, Barnes J, Liu Y (2001). "Catalytic activation of mitogen-activated protein (MAP) kinase phosphatase-1 by binding to p38 MAP kinase: critical role of the p38 C-terminal domain in its negative regulation.". Biochem. J. 352 Pt 1: 155–63. PMID 11062068.
Slack DN, Seternes OM, Gabrielsen M, Keyse SM (2001). "Distinct binding determinants for ERK2/p38alpha and JNK map kinases mediate catalytic activation and substrate selectivity of map kinase phosphatase-1.". J. Biol. Chem. 276 (19): 16491–500. doi:10.1074/jbc.M010966200. PMID 11278799.
Manzano RG, Montuenga LM, Dayton M, et al. (2002). "CL100 expression is down-regulated in advanced epithelial ovarian cancer and its re-expression decreases its malignant potential.". Oncogene 21 (28): 4435–47. doi:10.1038/sj.onc.1205542. PMID 12080474.
Imasato A, Desbois-Mouthon C, Han J, et al. (2003). "Inhibition of p38 MAPK by glucocorticoids via induction of MAPK phosphatase-1 enhances nontypeable Haemophilus influenzae-induced expression of toll-like receptor 2.". J. Biol. Chem. 277 (49): 47444–50. doi:10.1074/jbc.M208140200. PMID 12356755.
Lasa M, Abraham SM, Boucheron C, et al. (2002). "Dexamethasone causes sustained expression of mitogen-activated protein kinase (MAPK) phosphatase 1 and phosphatase-mediated inhibition of MAPK p38.". Mol. Cell. Biol. 22 (22): 7802–11. PMID 12391149.
Denkert C, Schmitt WD, Berger S, et al. (2002). "Expression of mitogen-activated protein kinase phosphatase-1 (MKP-1) in primary human ovarian carcinoma.". Int. J. Cancer 102 (5): 507–13. doi:10.1002/ijc.10746. PMID 12432554.