Biology:DUSP4
 Generic protein structure example |
Dual specificity protein phosphatase 4 is an enzyme that in humans is encoded by the DUSP4 gene.[1][2][3]
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, ERK2 and JNK, is expressed in a variety of tissues, and is localized in the nucleus. Two alternatively spliced transcript variants, encoding distinct isoforms, have been observed for this gene. In addition, multiple polyadenylation sites have been reported.[3]
In melanocytic cells DUSP4 gene expression may be regulated by MITF.[4]
References
- ↑ "Isolation and characterization of a novel dual specific phosphatase, HVH2, which selectively dephosphorylates the mitogen-activated protein kinase". The Journal of Biological Chemistry 270 (13): 7197–203. Mar 1995. doi:10.1074/jbc.270.13.7197. PMID 7535768.
- ↑ "Chromosomal localization of three human dual specificity phosphatase genes (DUSP4, DUSP6, and DUSP7)". Genomics 42 (3): 524–7. Jun 1997. doi:10.1006/geno.1997.4756. PMID 9205128.
- ↑ 3.0 3.1 "Entrez Gene: DUSP4 dual specificity phosphatase 4". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1846.
- ↑ "Novel MITF targets identified using a two-step DNA microarray strategy". Pigment Cell & Melanoma Research 21 (6): 665–76. Dec 2008. doi:10.1111/j.1755-148X.2008.00505.x. PMID 19067971.
Further reading
- "Isolation and characterisation of a uniquely regulated threonine, tyrosine phosphatase (TYP 1) which inactivates ERK2 and p54jnk". Oncogene 11 (12): 2553–63. Dec 1995. PMID 8545112.
- "The mitogen-activated protein kinase phosphatases PAC1, MKP-1, and MKP-2 have unique substrate specificities and reduced activity in vivo toward the ERK2 sevenmaker mutation". The Journal of Biological Chemistry 271 (11): 6497–501. Mar 1996. doi:10.1074/jbc.271.11.6497. PMID 8626452.
- "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Research 6 (9): 791–806. Sep 1996. doi:10.1101/gr.6.9.791. PMID 8889548.
- "Proteomic analysis of NMDA receptor-adhesion protein signaling complexes". Nature Neuroscience 3 (7): 661–9. Jul 2000. doi:10.1038/76615. PMID 10862698.
- "Discordance between the binding affinity of mitogen-activated protein kinase subfamily members for MAP kinase phosphatase-2 and their ability to activate the phosphatase catalytically". The Journal of Biological Chemistry 276 (31): 29440–9. Aug 2001. doi:10.1074/jbc.M103463200. PMID 11387337.
- "Conditional expression of MAP kinase phosphatase-2 protects against genotoxic stress-induced apoptosis by binding and selective dephosphorylation of nuclear activated c-jun N-terminal kinase". Cellular Signalling 17 (10): 1254–64. Oct 2005. doi:10.1016/j.cellsig.2005.01.003. PMID 16038800.
- "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. Oct 2005. doi:10.1038/nature04209. PMID 16189514. Bibcode: 2005Natur.437.1173R.
- "Modulation of replicative senescence of diploid human cells by nuclear ERK signaling". The Journal of Biological Chemistry 282 (6): 4136–51. Feb 2007. doi:10.1074/jbc.M604955200. PMID 17145763.
- "A molecular link between E2F-1 and the MAPK cascade". The Journal of Biological Chemistry 282 (25): 18521–31. Jun 2007. doi:10.1074/jbc.M610538200. PMID 17452331.
External links
- Overview of all the structural information available in the PDB for UniProt: Q13115 (Human Dual specificity protein phosphatase 4) at the PDBe-KB.
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