Dual specificity phosphatase: Difference between revisions
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{{STRUCTURE_1ohe| PDB=1ohe | SIZE=400 | SCENE= |right|CAPTION=Human Cdc14B2 core domain (grey) complex with tripeptide (green) and acetyl (PDB code [[1ohe]]). }} | {{STRUCTURE_1ohe| PDB=1ohe | SIZE=400 | SCENE= |right|CAPTION=Human Cdc14B2 core domain (grey) complex with tripeptide (green) and acetyl (PDB code [[1ohe]]). }} | ||
== Function == | |||
'''Dual specificity phosphatase''' (DUSP) is a phosphatase which acts on tyrosine, serine or threonine residues. There are several DUSP enzymes in mammals sharing a common catalytic mechanism. The DUSP include:<br /> | '''Dual specificity phosphatase''' (DUSP) is a phosphatase which acts on tyrosine, serine or threonine residues. There are several DUSP enzymes in mammals sharing a common catalytic mechanism. The DUSP include:<br /> | ||
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• Myotubularin<ref>PMID:12847286</ref><br /> | • Myotubularin<ref>PMID:12847286</ref><br /> | ||
• MAPK phosphatase see [[MAP kinase phosphatase]]<br /> | • MAPK phosphatase see [[MAP kinase phosphatase]]<br /> | ||
== Relevance == | |||
Cdc25A and Cdc25B are overexpressed in several types of cancers and their inhibitors are being tested as chemotherapeutic agents. | |||
==3D structures of dual specificity phosphatase== | ==3D structures of dual specificity phosphatase== | ||
Revision as of 17:31, 3 January 2016
FunctionFunction
Dual specificity phosphatase (DUSP) is a phosphatase which acts on tyrosine, serine or threonine residues. There are several DUSP enzymes in mammals sharing a common catalytic mechanism. The DUSP include:
• Slingshot phosphatase[1]
• Phosphatase of regenerating liver[2]
• Cdc14[3]
• Cdc25[4]
• PTEN[5]
• Myotubularin[6]
• MAPK phosphatase see MAP kinase phosphatase
RelevanceRelevance
Cdc25A and Cdc25B are overexpressed in several types of cancers and their inhibitors are being tested as chemotherapeutic agents.
3D structures of dual specificity phosphatase3D structures of dual specificity phosphatase
Updated on 03-January-2016
ReferencesReferences
- ↑ Kligys K, Claiborne JN, DeBiase PJ, Hopkinson SB, Wu Y, Mizuno K, Jones JC. The slingshot family of phosphatases mediates Rac1 regulation of cofilin phosphorylation, laminin-332 organization, and motility behavior of keratinocytes. J Biol Chem. 2007 Nov 2;282(44):32520-8. Epub 2007 Sep 11. PMID:17848544 doi:http://dx.doi.org/10.1074/jbc.M707041200
- ↑ Walls CD, Iliuk A, Bai Y, Wang M, Tao WA, Zhang ZY. Phosphatase of regenerating liver 3 (PRL3) provokes a tyrosine phosphoproteome to drive prometastatic signal transduction. Mol Cell Proteomics. 2013 Dec;12(12):3759-77. doi: 10.1074/mcp.M113.028886. Epub , 2013 Sep 12. PMID:24030100 doi:http://dx.doi.org/10.1074/mcp.M113.028886
- ↑ Stegmeier F, Amon A. Closing mitosis: the functions of the Cdc14 phosphatase and its regulation. Annu Rev Genet. 2004;38:203-32. PMID:15568976 doi:http://dx.doi.org/10.1146/annurev.genet.38.072902.093051
- ↑ Kristjansdottir K, Rudolph J. Cdc25 phosphatases and cancer. Chem Biol. 2004 Aug;11(8):1043-51. PMID:15324805 doi:http://dx.doi.org/10.1016/j.chembiol.2004.07.007
- ↑ Lee JO, Yang H, Georgescu MM, Di Cristofano A, Maehama T, Shi Y, Dixon JE, Pandolfi P, Pavletich NP. Crystal structure of the PTEN tumor suppressor: implications for its phosphoinositide phosphatase activity and membrane association. Cell. 1999 Oct 29;99(3):323-34. PMID:10555148
- ↑ Nandurkar HH, Layton M, Laporte J, Selan C, Corcoran L, Caldwell KK, Mochizuki Y, Majerus PW, Mitchell CA. Identification of myotubularin as the lipid phosphatase catalytic subunit associated with the 3-phosphatase adapter protein, 3-PAP. Proc Natl Acad Sci U S A. 2003 Jul 22;100(15):8660-5. Epub 2003 Jul 7. PMID:12847286 doi:http://dx.doi.org/10.1073/pnas.1033097100