Dual specificity phosphatase: Difference between revisions

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Michal Harel, Jaime Prilusky, Alexander Berchansky, Joel L. Sussman

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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]]). }}
+<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]]).'>
-'''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 />
+== Function ==
-•	Slingshot phosphatase<br />
-•	Phosphatase of regenerating liver<br />
-•	Cdc14<br />
-•	Cdc25<br />
-•	PTEN<br />
-•	Myotubularin<br />
-•	MAPK phosphatase see [[MAP kinase phosphatase]]<br />
-==3D structures of dual specificity phosphatase==
+'''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 />
+•	'''Phosphatase of regenerating liver''' (PRL)<ref>PMID:24030100</ref><br />
+•	'''Cdc14''' leads to mitotic exit by dephosphorylation of targets of the protein kinase Cdk1.<ref>PMID:15568976</ref><br />
+•	'''Cdc25''' activates Cdk1 by its dephosphorylation.<ref>PMID:15324805</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 />
+•	'''MAPK phosphatase''' see [[MAP kinase phosphatase]]<br />
-Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
+== Relevance ==
-{{#tree:id=OrganizedByTopic|openlevels=0|
-*Slingshot phosphatase (SSH)
+'''Cdc25A''' and '''Cdc25B''' are overexpressed in several types of cancers and their inhibitors are being tested as chemotherapeutic agents.<br />
+'''PTEN''' gene is mutated with high frequency in a variety of human cancers.<ref>PMID:18298792</ref><br />
+'''Phosphatase of regenerating liver''' is overexpressed in several types of cancers.
-**[[2nt2]]  – hSSH-2L catalytic domain - human<br />
+== Disease ==
-*Phosphatase of regenerating liver (RPL)
+Myotubularin mutations are responsible for the hereditary motor disease Charcot-Marie-Tooth disease.<ref>PMID:12045210</ref>
-**[[1xm2]]  – hPRL-1 (mutant)<br />
+== Structural highlights ==
-**[[1zck]], [[1x24]]  – rPRL-1 - rat<br />
-**[[1zcl]] – rPRL-1 (mutant)<br />
-**[[1r6h]], [[1v3a]], [[2mbc]]  – hPRL-3 - NMR<br />
-*Cdc14
+<scene name='44/444621/Cv/6'>Tripeptide binding site</scene> in human Cdc14B2 (PDB code [[1ohe]]).<ref>PMID:12853468</ref>
-**[[1ohc]], [[1ohd]]  – hCdc14B2 core domain <br />
+==3D structures of dual specificity phosphatase==
-**[[1ohe]]  – hCdc14B2 core domain + peptide<br />
+[[Dual specificity phosphatase 3D structures]]
-*Cdc25
-**[[1qb0]], [[1cwr]], [[1cws]], [[1cwt]], [[1ym9]], [[1ymd]], [[1ymk]], [[1yml]], [[1ys0]], [[2uzq]]  – hCdc25B catalytic domain <br />
-**[[2a2k]], [[2ifd]], [[2ifv]]  – hCdc25B catalytic domain (mutant)<br />
-*Phosphoinositide phosphatase PTEN
-**[[1d5r]] – hPTEN (mutant)<br />
-*Myotubularin-related protein (MTMR)
-**[[1zvr]] – hMTMR2 PH-gram and phosphatase domains (mutant)<br />
+</StructureSection>
-**[[1zsq]] - hMTMR2 PH-gram and phosphatase domains (mutant) + phosphatidylinositol 3-phosphate<br />
-**[[1m7r]], [[1lw3]] - hMTMR2 PH-gram and phosphatase domains (mutant) + phosphate<br />
-**[[2yf0]] – hMTMR6<br />
-*MAPK phosphatase see [[MAP kinase phosphatase]]
+== References ==
-}}
+<references/>
 [[Category:Topic Page]]