Dual specificity phosphatase: Difference between revisions
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<StructureSection load='' size='350' side='right' scene='44/444621/Cv/1' caption='Human Cdc14B2 core domain (cyan) complex with tripeptide (green) and acetyl (PDB code [[1ohe]]).'> | |||
== Function == | == Function == | ||
'''Dual specificity phosphatase''' (DUSP) is a phosphatase which | '''Dual specificity phosphatase''' or '''Dual specificity protein phosphatase''' (DUSP) is a phosphatase which dephosphorylates phosphotyrosine, phosphoserine or phosphothreonine residues<ref>PMID:19228121</ref>. There are several DUSP enzymes in mammals sharing a common catalytic mechanism. The DUSP include:<br /> | ||
• '''Slingshot phosphatase'''<ref>PMID:17848544</ref><br /> | • '''Slingshot phosphatase'''<ref>PMID:17848544</ref><br /> | ||
• '''Phosphatase of regenerating liver''' (PRL)<ref>PMID:24030100</ref><br /> | • '''Phosphatase of regenerating liver''' (PRL)<ref>PMID:24030100</ref><br /> | ||
• '''Cdc14'''<ref>PMID:15568976</ref><br /> | • '''Cdc14''' leads to mitotic exit by dephosphorylation of targets of the protein kinase Cdk1.<ref>PMID:15568976</ref><br /> | ||
• '''Cdc25'''<ref>PMID:15324805</ref><br /> | • '''Cdc25''' activates Cdk1 by its dephosphorylation.<ref>PMID:15324805</ref><br /> | ||
• '''PTEN'''<ref>PMID:10555148</ref><br /> | • '''PTEN''' (Phosphatase and TEnsin homolog) dephosphorylates phosphasitide substrates.<ref>PMID:10555148</ref> For details see [[PTEN]].<br /> | ||
• '''Myotubularin''' dephosphorylates phosphadinylinositol 3-phosphate and phosphadinylinositol (3,5)-bi-phosphate<ref>PMID:12847286</ref><br /> | • '''Myotubularin''' dephosphorylates phosphadinylinositol 3-phosphate and phosphadinylinositol (3,5)-bi-phosphate<ref>PMID:12847286</ref><br /> | ||
• '''MAPK phosphatase''' see [[MAP kinase phosphatase]]<br /> | • '''MAPK phosphatase''' see [[MAP kinase phosphatase]]<br /> | ||
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Myotubularin mutations are responsible for the hereditary motor disease Charcot-Marie-Tooth disease.<ref>PMID:12045210</ref> | Myotubularin mutations are responsible for the hereditary motor disease Charcot-Marie-Tooth disease.<ref>PMID:12045210</ref> | ||
== | == Structural highlights == | ||
<scene name='44/444621/Cv/6'>Tripeptide binding site</scene> in human Cdc14B2 (PDB code [[1ohe]]).<ref>PMID:12853468</ref> | |||
==3D structures of dual specificity phosphatase== | |||
[[Dual specificity phosphatase 3D structures]] | |||
</StructureSection> | |||
== References == | == References == | ||
<references/> | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Latest revision as of 10:17, 11 July 2021
FunctionDual specificity phosphatase or Dual specificity protein phosphatase (DUSP) is a phosphatase which dephosphorylates phosphotyrosine, phosphoserine or phosphothreonine residues[1]. There are several DUSP enzymes in mammals sharing a common catalytic mechanism. The DUSP include: • Slingshot phosphatase[2] RelevanceCdc25A and Cdc25B are overexpressed in several types of cancers and their inhibitors are being tested as chemotherapeutic agents. PTEN gene is mutated with high frequency in a variety of human cancers.[8] DiseaseMyotubularin mutations are responsible for the hereditary motor disease Charcot-Marie-Tooth disease.[9] Structural highlightsin human Cdc14B2 (PDB code 1ohe).[10] 3D structures of dual specificity phosphataseDual specificity phosphatase 3D structures
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ReferencesReferences
- ↑ Patterson KI, Brummer T, O'Brien PM, Daly RJ. Dual-specificity phosphatases: critical regulators with diverse cellular targets. Biochem J. 2009 Mar 15;418(3):475-89. doi: 10.1042/bj20082234. PMID:19228121 doi:http://dx.doi.org/10.1042/bj20082234
- ↑ 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
- ↑ Pulido R, Hooft van Huijsduijnen R. Protein tyrosine phosphatases: dual-specificity phosphatases in health and disease. FEBS J. 2008 Mar;275(5):848-66. doi: 10.1111/j.1742-4658.2008.06250.x. PMID:18298792 doi:http://dx.doi.org/10.1111/j.1742-4658.2008.06250.x
- ↑ Berger P, Bonneick S, Willi S, Wymann M, Suter U. Loss of phosphatase activity in myotubularin-related protein 2 is associated with Charcot-Marie-Tooth disease type 4B1. Hum Mol Genet. 2002 Jun 15;11(13):1569-79. PMID:12045210
- ↑ Gray CH, Good VM, Tonks NK, Barford D. The structure of the cell cycle protein Cdc14 reveals a proline-directed protein phosphatase. EMBO J. 2003 Jul 15;22(14):3524-35. PMID:12853468 doi:10.1093/emboj/cdg348