Protein tyrosine phosphatases: dual-specificity phosphatases in health and disease
Dual-specificity phosphatases (DSPs) constitute a subfamily of protein tyrosine phosphatases (PTPs) that dephosphorylates phospho-Tyr, phospho-Ser and nonproteinaceous substrates. DSPs are involved in the regulation of both developmental and postnatal essential processes, such as early embryogenesis...
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| Veröffentlicht in: | The FEBS journal 2008-03, Vol.275 (5), p.848-866 |
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| creator | Pulido, Rafael van Huijsduijnen, Rob Hooft |
| description | Dual-specificity phosphatases (DSPs) constitute a subfamily of protein tyrosine phosphatases (PTPs) that dephosphorylates phospho-Tyr, phospho-Ser and nonproteinaceous substrates. DSPs are involved in the regulation of both developmental and postnatal essential processes, such as early embryogenesis, placental development and immune responses. Several DSP genes are implicated in familial and sporadic human diseases, including tumor-related, neurological and muscle disorders, and cardiovascular and inflammatory diseases. This association ranges from disease-causative mutations to disease-risk-prone single-nucleotide polymorphisms, promoter methylation or gene duplication (most often in cancer). Deconvolution of the role of DSPs in disease is challenging. The enzymes' activities are regulated at many levels and they form part of extensive, intricate networks with other signaling components. Here, we review current knowledge of the role of cysteine-based PTP-domain DSPs in health and disease, and their suitability as putative therapeutic targets for drugs is discussed. |
| doi_str_mv | 10.1111/j.1742-4658.2008.06250.x |
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Here, we review current knowledge of the role of cysteine-based PTP-domain DSPs in health and disease, and their suitability as putative therapeutic targets for drugs is discussed.</description><subject>Animals</subject><subject>arthritis</subject><subject>asthma</subject><subject>Biochemistry</subject><subject>cancer</subject><subject>Dual-Specificity Phosphatases - antagonists & inhibitors</subject><subject>Dual-Specificity Phosphatases - genetics</subject><subject>Dual-Specificity Phosphatases - metabolism</subject><subject>Enzyme Inhibitors - pharmacology</subject><subject>Enzyme Inhibitors - therapeutic use</subject><subject>Genetics</subject><subject>Humans</subject><subject>Immunology</subject><subject>laforin</subject><subject>Mice</subject><subject>multiple sclerosis</subject><subject>myoclonus epilepsy</subject><subject>myotubular myopathy</subject><subject>Prenatal development</subject><subject>protein phosphorylation/dephosphorylation</subject><subject>Proteins</subject><subject>PTEN</subject><subject>Rats</subject><subject>signal transduction</subject><subject>Substrates</subject><issn>1742-464X</issn><issn>1742-4658</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkMtKxDAUhoMo3l9Biwt3rSe3NnEhqHgDQXEU3IU0kzoZOm1tWnTe3tQZRnRlNjnkfP9P-BCKMCQ4nJNpgjNGYpZykRAAkUBKOCSfa2h7tVhfzex1C-14PwWgnEm5ibawIFJkkmyjp8e27qyrom7e1t5VNmomtW8mutPe-tNo3Osy9o01rnDGdfNf6yjkJlaX3STS1TgaO2_D8x7aKHTp7f7y3kUv11fPl7fx_cPN3eX5fWw45RBLnREqiAGhoaDA85wwQnjGdZoDZzjNGTPaAMFEGMFTEIznVjJdaCOkzOkuOl70Nm393lvfqZnzxpalrmzde5UBpZxmOIBHf8Bp3bdV-JsiwDBhIFmAxAIywYNvbaGa1s10O1cY1CBdTdXgUw1u1SBdfUtXnyF6sOzv85kd_wSXlgNwtgA-XGnn_y5W11cXo2EMBYeLgkLXSr-1zquXEQFMA83TlAH9AidzmP0</recordid><startdate>200803</startdate><enddate>200803</enddate><creator>Pulido, Rafael</creator><creator>van Huijsduijnen, Rob Hooft</creator><general>Oxford, UK : Blackwell Publishing Ltd</general><general>Blackwell Publishing Ltd</general><scope>FBQ</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>200803</creationdate><title>Protein tyrosine phosphatases: dual-specificity phosphatases in health and disease</title><author>Pulido, Rafael ; van Huijsduijnen, Rob Hooft</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5350-9a72382c08a0f305bb2422575a6b05416b44cac02128c8560845be94afac899b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Animals</topic><topic>arthritis</topic><topic>asthma</topic><topic>Biochemistry</topic><topic>cancer</topic><topic>Dual-Specificity Phosphatases - antagonists & inhibitors</topic><topic>Dual-Specificity Phosphatases - genetics</topic><topic>Dual-Specificity Phosphatases - metabolism</topic><topic>Enzyme Inhibitors - pharmacology</topic><topic>Enzyme Inhibitors - therapeutic use</topic><topic>Genetics</topic><topic>Humans</topic><topic>Immunology</topic><topic>laforin</topic><topic>Mice</topic><topic>multiple sclerosis</topic><topic>myoclonus epilepsy</topic><topic>myotubular myopathy</topic><topic>Prenatal development</topic><topic>protein phosphorylation/dephosphorylation</topic><topic>Proteins</topic><topic>PTEN</topic><topic>Rats</topic><topic>signal transduction</topic><topic>Substrates</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Pulido, Rafael</creatorcontrib><creatorcontrib>van Huijsduijnen, Rob Hooft</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>The FEBS journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Pulido, Rafael</au><au>van Huijsduijnen, Rob Hooft</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Protein tyrosine phosphatases: dual-specificity phosphatases in health and disease</atitle><jtitle>The FEBS journal</jtitle><addtitle>FEBS J</addtitle><date>2008-03</date><risdate>2008</risdate><volume>275</volume><issue>5</issue><spage>848</spage><epage>866</epage><pages>848-866</pages><issn>1742-464X</issn><eissn>1742-4658</eissn><abstract>Dual-specificity phosphatases (DSPs) constitute a subfamily of protein tyrosine phosphatases (PTPs) that dephosphorylates phospho-Tyr, phospho-Ser and nonproteinaceous substrates. 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| subjects | Animals arthritis asthma Biochemistry cancer Dual-Specificity Phosphatases - antagonists & inhibitors Dual-Specificity Phosphatases - genetics Dual-Specificity Phosphatases - metabolism Enzyme Inhibitors - pharmacology Enzyme Inhibitors - therapeutic use Genetics Humans Immunology laforin Mice multiple sclerosis myoclonus epilepsy myotubular myopathy Prenatal development protein phosphorylation/dephosphorylation Proteins PTEN Rats signal transduction Substrates |
| title | Protein tyrosine phosphatases: dual-specificity phosphatases in health and disease |
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