Dual specificity phosphatase

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== Function ==
== Function ==
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'''Dual specificity 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 />
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'''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 />
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</StructureSection>
</StructureSection>
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==3D structures of dual specificity phosphatase==
 
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
 
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{{#tree:id=OrganizedByTopic|openlevels=0|
 
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*Dual specificity phosphatase
 
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**[[4y2e]] – hDUSP 7 catalytic domain (mutant) - human<br />
 
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**[[5xjv]] – hDUSP 13A (mutant) <br />
 
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**[[4yr8]] – hDUSP 16 residues 156-301 + MAPK 8<br />
 
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**[[4woh]] – hDUSP 22 (mutant) + nitrophenolphosphate<br />
 
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**[[5gtj]] – hDUSP 26 (mutant) <br />
 
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**[[5y15]], [[5y16]] – hDUSP 28 (mutant) <br />
 
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*Slingshot phosphatase (SSH)
 
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**[[2nt2]] – hSSH-2L catalytic domain - human<br />
 
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*Phosphatase of regenerating liver (PRL) or protein tyrosine phosphatase type IVA
 
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**[[1rxd]] – hPRL-1 <br />
 
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**[[1xm2]] – hPRL-1 (mutant)<br />
 
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**[[5bx1]] – hPRL-1 + inhibitor<br />
 
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**[[1zck]], [[1x24]] – rPRL-1 - rat<br />
 
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**[[1zcl]] – rPRL-1 (mutant)<br />
 
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**[[3rz2]] – rPRL-1 + peptide<br />
 
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**[[5mmz]], [[5lxq]] – mPRL-1 + magnesium transporter - mouse<br />
 
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**[[5k24]] – mPRL-2 + magnesium transporter<br />
 
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**[[5k25]], [[5k23]] – hPRL-2 + magnesium transporter<br />
 
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**[[5k22]] – hPRL-2 (mutant) + magnesium transporter<br />
 
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**[[1r6h]], [[1v3a]], [[2mbc]] – hPRL-3 - NMR<br />
 
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**[[5tsr]] – hPRL-3 + magnesium transporter<br />
 
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*Cdc14
 
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**[[1ohc]], [[1ohd]] – hCdc14B2 core domain <br />
 
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**[[1ohe]] – hCdc14B2 core domain + peptide<br />
 
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**[[6g86]] – hCdc14 + SIC1 peptide<br />
 
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**[[6g85]], [[6g84]] – hCdc14 + CBK1 peptide<br />
 
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**[[5xw5]] – hCdc14 + SWI6P peptide<br />
 
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**[[5xw4]] – yCdc14 - yeast<br />
 
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**[[4zj7]] – yCdc14 C-terminal + importin<br />
 
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*Cdc25
 
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**[[1qb0]], [[1cwr]], [[1cws]], [[1cwt]], [[1ym9]], [[1ymd]], [[1ymk]], [[1yml]], [[1ys0]], [[2uzq]] – hCdc25B catalytic domain <br />
 
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**[[2a2k]], [[2ifd]], [[2ifv]] – hCdc25B catalytic domain (mutant)<br />
 
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*Phosphoinositide phosphatase PTEN
 
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**[[1d5r]], [[5bzz]], [[5bzx]], [[5bug]] – hPTEN (mutant)<br />
 
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*Phosphoinositide phosphatase Sac1
 
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**[[3lwt]] – ySac1<br />
 
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**[[4tu3]] – ySac1 + VPS74<br />
 
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*Phosphoinositide phosphatase Sac2
 
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**[[4xuu]] – hSac2 residues 169-563<br />
 
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*Myotubularin-related protein (MTMR)
 
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**[[1zvr]] – hMTMR2 PH-gram and phosphatase domains (mutant)<br />
 
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**[[1zsq]] - hMTMR2 PH-gram and phosphatase domains (mutant) + phosphatidylinositol 3-phosphate<br />
 
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**[[1m7r]], [[1lw3]] - hMTMR2 PH-gram and phosphatase domains (mutant) + phosphate<br />
 
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**[[2yf0]] – hMTMR6<br />
 
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Myotubularin-related protein 15 (MTMR15) or Fanconi-associated nuclease 1
 
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**[[4rid]], [[4ry3]] – hMTMR15 residues 370-1009<br />
 
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**[[4rec]], [[4ri8]], [[4ri9]], [[4ria]], [[4rib]], [[4ric]], [[4reb]], [[4rea]] – hMTMR15 (mutant) + DNA<br />
 
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*MAPK phosphatase see [[MAP kinase phosphatase]]
 
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}}
 
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

Human Cdc14B2 core domain (cyan) complex with tripeptide (green) and acetyl (PDB code 1ohe).

Drag the structure with the mouse to rotate

References

  1. ↑ 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
  2. ↑ 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
  3. ↑ 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
  4. ↑ 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
  5. ↑ 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
  6. ↑ 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
  7. ↑ 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
  8. ↑ 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
  9. ↑ 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
  10. ↑ 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

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