voltage-sensing phosphatase, Ci-VSP, which shares sequence identity with PTEN, dephosphorylates phosphatidylinositol 4,5-bisphosphate
Phosphatidylinositol lipids play diverse physiological roles, and their concentrations are tightly regulated by various kinases and phosphatases. The enzymatic activity of Ciona intestinalis voltage sensor-containing phosphatase (Ci-VSP), recently identified as a member of the PTEN (phosphatase and...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2008-06, Vol.105 (23), p.7970-7975 |
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| creator | Iwasaki, Hirohide Murata, Yoshimichi Kim, Youngjun Hossain, Md. Israil Worby, Carolyn A Dixon, Jack E McCormack, Thomas Sasaki, Takehiko Okamura, Yasushi |
| description | Phosphatidylinositol lipids play diverse physiological roles, and their concentrations are tightly regulated by various kinases and phosphatases. The enzymatic activity of Ciona intestinalis voltage sensor-containing phosphatase (Ci-VSP), recently identified as a member of the PTEN (phosphatase and tensin homolog deleted on chromosome 10) family of phosphatidylinositol phosphatases, is regulated by its own voltage-sensor domain in a voltage-dependent manner. However, a detailed mechanism of Ci-VSP regulation and its substrate specificity remain unknown. Here we determined the in vitro substrate specificity of Ci-VSP by measuring the phosphoinositide phosphatase activity of the Ci-VSP cytoplasmic phosphatase domain. Despite the high degree of identity shared between the active sites of PTEN and Ci-VSP, Ci-VSP dephosphorylates not only the PTEN substrate, phosphatidylinositol 3,4,5-trisphosphate [PI(3,4,5)P₃], but also, unlike PTEN, phosphatidylinositol 4,5-bisphosphate [PI(4,5)P₂]. Enzymatic action on PI(4,5)P₂ removes the phosphate at position 5 of the inositol ring, resulting in the production of phosphatidylinositol 4-phosphate [PI(4)P]. The active site Cys-X₅-Arg (CX₅R) sequence of Ci-VSP differs with that of PTEN only at amino acid 365 where a glycine residue in Ci-VSP is replaced by an alanine in PTEN. Ci-VSP with a G365A mutation no longer dephosphorylates PI(4,5)P₂ and is not capable of inducing depolarization-dependent rundown of a PI(4,5)P₂-dependent potassium channel. These results indicate that Ci-VSP is a PI(3,4,5)P₃/PI(4,5)P₂ phosphatase that uniquely functions in the voltage-dependent regulation of ion channels through regulation of PI(4,5)P₂ levels. |
| doi_str_mv | 10.1073/pnas.0803936105 |
| format | Article |
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Israil ; Worby, Carolyn A ; Dixon, Jack E ; McCormack, Thomas ; Sasaki, Takehiko ; Okamura, Yasushi</creator><creatorcontrib>Iwasaki, Hirohide ; Murata, Yoshimichi ; Kim, Youngjun ; Hossain, Md. Israil ; Worby, Carolyn A ; Dixon, Jack E ; McCormack, Thomas ; Sasaki, Takehiko ; Okamura, Yasushi</creatorcontrib><description>Phosphatidylinositol lipids play diverse physiological roles, and their concentrations are tightly regulated by various kinases and phosphatases. The enzymatic activity of Ciona intestinalis voltage sensor-containing phosphatase (Ci-VSP), recently identified as a member of the PTEN (phosphatase and tensin homolog deleted on chromosome 10) family of phosphatidylinositol phosphatases, is regulated by its own voltage-sensor domain in a voltage-dependent manner. However, a detailed mechanism of Ci-VSP regulation and its substrate specificity remain unknown. Here we determined the in vitro substrate specificity of Ci-VSP by measuring the phosphoinositide phosphatase activity of the Ci-VSP cytoplasmic phosphatase domain. Despite the high degree of identity shared between the active sites of PTEN and Ci-VSP, Ci-VSP dephosphorylates not only the PTEN substrate, phosphatidylinositol 3,4,5-trisphosphate [PI(3,4,5)P₃], but also, unlike PTEN, phosphatidylinositol 4,5-bisphosphate [PI(4,5)P₂]. Enzymatic action on PI(4,5)P₂ removes the phosphate at position 5 of the inositol ring, resulting in the production of phosphatidylinositol 4-phosphate [PI(4)P]. The active site Cys-X₅-Arg (CX₅R) sequence of Ci-VSP differs with that of PTEN only at amino acid 365 where a glycine residue in Ci-VSP is replaced by an alanine in PTEN. Ci-VSP with a G365A mutation no longer dephosphorylates PI(4,5)P₂ and is not capable of inducing depolarization-dependent rundown of a PI(4,5)P₂-dependent potassium channel. These results indicate that Ci-VSP is a PI(3,4,5)P₃/PI(4,5)P₂ phosphatase that uniquely functions in the voltage-dependent regulation of ion channels through regulation of PI(4,5)P₂ levels.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.0803936105</identifier><identifier>PMID: 18524949</identifier><language>eng</language><publisher>United States: National Academy of Sciences</publisher><subject>Amino Acid Sequence ; Amino Acid Substitution ; Amino acids ; Animals ; Binding Sites ; Biological Sciences ; Ciona intestinalis ; Ciona intestinalis - enzymology ; Depolarization ; Electric current ; Electric potential ; Glycine - metabolism ; Inositols ; Ion Channel Gating ; Ion channels ; Ion Channels - metabolism ; Kinases ; Lipids ; Molecular Sequence Data ; Mutant Proteins - metabolism ; Mutation ; Oocytes ; Phosphatases ; Phosphates ; Phosphatidylinositol 4,5-Diphosphate - metabolism ; Phosphatidylinositols ; Phosphoric Monoester Hydrolases - chemistry ; Phosphoric Monoester Hydrolases - metabolism ; Phosphorylation ; PTEN Phosphohydrolase - chemistry ; Sequence Homology, Amino Acid ; Substrate Specificity ; Xenopus</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 2008-06, Vol.105 (23), p.7970-7975</ispartof><rights>Copyright 2008 The National Academy of Sciences of the United States of America</rights><rights>Copyright National Academy of Sciences Jun 10, 2008</rights><rights>2008 by The National Academy of Sciences of the USA</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c552t-bb409efb4c8a646097dbbab4ae6cb32ec6b4823f4eed45a85effacc4241625a63</citedby><cites>FETCH-LOGICAL-c552t-bb409efb4c8a646097dbbab4ae6cb32ec6b4823f4eed45a85effacc4241625a63</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/105/23.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/25462715$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/25462715$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,315,728,781,785,804,886,27929,27930,53796,53798,58022,58255</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18524949$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Iwasaki, Hirohide</creatorcontrib><creatorcontrib>Murata, Yoshimichi</creatorcontrib><creatorcontrib>Kim, Youngjun</creatorcontrib><creatorcontrib>Hossain, Md. Israil</creatorcontrib><creatorcontrib>Worby, Carolyn A</creatorcontrib><creatorcontrib>Dixon, Jack E</creatorcontrib><creatorcontrib>McCormack, Thomas</creatorcontrib><creatorcontrib>Sasaki, Takehiko</creatorcontrib><creatorcontrib>Okamura, Yasushi</creatorcontrib><title>voltage-sensing phosphatase, Ci-VSP, which shares sequence identity with PTEN, dephosphorylates phosphatidylinositol 4,5-bisphosphate</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>Phosphatidylinositol lipids play diverse physiological roles, and their concentrations are tightly regulated by various kinases and phosphatases. The enzymatic activity of Ciona intestinalis voltage sensor-containing phosphatase (Ci-VSP), recently identified as a member of the PTEN (phosphatase and tensin homolog deleted on chromosome 10) family of phosphatidylinositol phosphatases, is regulated by its own voltage-sensor domain in a voltage-dependent manner. However, a detailed mechanism of Ci-VSP regulation and its substrate specificity remain unknown. Here we determined the in vitro substrate specificity of Ci-VSP by measuring the phosphoinositide phosphatase activity of the Ci-VSP cytoplasmic phosphatase domain. Despite the high degree of identity shared between the active sites of PTEN and Ci-VSP, Ci-VSP dephosphorylates not only the PTEN substrate, phosphatidylinositol 3,4,5-trisphosphate [PI(3,4,5)P₃], but also, unlike PTEN, phosphatidylinositol 4,5-bisphosphate [PI(4,5)P₂]. Enzymatic action on PI(4,5)P₂ removes the phosphate at position 5 of the inositol ring, resulting in the production of phosphatidylinositol 4-phosphate [PI(4)P]. The active site Cys-X₅-Arg (CX₅R) sequence of Ci-VSP differs with that of PTEN only at amino acid 365 where a glycine residue in Ci-VSP is replaced by an alanine in PTEN. Ci-VSP with a G365A mutation no longer dephosphorylates PI(4,5)P₂ and is not capable of inducing depolarization-dependent rundown of a PI(4,5)P₂-dependent potassium channel. 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Israil</au><au>Worby, Carolyn A</au><au>Dixon, Jack E</au><au>McCormack, Thomas</au><au>Sasaki, Takehiko</au><au>Okamura, Yasushi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>voltage-sensing phosphatase, Ci-VSP, which shares sequence identity with PTEN, dephosphorylates phosphatidylinositol 4,5-bisphosphate</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>2008-06-10</date><risdate>2008</risdate><volume>105</volume><issue>23</issue><spage>7970</spage><epage>7975</epage><pages>7970-7975</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>Phosphatidylinositol lipids play diverse physiological roles, and their concentrations are tightly regulated by various kinases and phosphatases. The enzymatic activity of Ciona intestinalis voltage sensor-containing phosphatase (Ci-VSP), recently identified as a member of the PTEN (phosphatase and tensin homolog deleted on chromosome 10) family of phosphatidylinositol phosphatases, is regulated by its own voltage-sensor domain in a voltage-dependent manner. However, a detailed mechanism of Ci-VSP regulation and its substrate specificity remain unknown. Here we determined the in vitro substrate specificity of Ci-VSP by measuring the phosphoinositide phosphatase activity of the Ci-VSP cytoplasmic phosphatase domain. Despite the high degree of identity shared between the active sites of PTEN and Ci-VSP, Ci-VSP dephosphorylates not only the PTEN substrate, phosphatidylinositol 3,4,5-trisphosphate [PI(3,4,5)P₃], but also, unlike PTEN, phosphatidylinositol 4,5-bisphosphate [PI(4,5)P₂]. Enzymatic action on PI(4,5)P₂ removes the phosphate at position 5 of the inositol ring, resulting in the production of phosphatidylinositol 4-phosphate [PI(4)P]. The active site Cys-X₅-Arg (CX₅R) sequence of Ci-VSP differs with that of PTEN only at amino acid 365 where a glycine residue in Ci-VSP is replaced by an alanine in PTEN. Ci-VSP with a G365A mutation no longer dephosphorylates PI(4,5)P₂ and is not capable of inducing depolarization-dependent rundown of a PI(4,5)P₂-dependent potassium channel. These results indicate that Ci-VSP is a PI(3,4,5)P₃/PI(4,5)P₂ phosphatase that uniquely functions in the voltage-dependent regulation of ion channels through regulation of PI(4,5)P₂ levels.</abstract><cop>United States</cop><pub>National Academy of Sciences</pub><pmid>18524949</pmid><doi>10.1073/pnas.0803936105</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Amino Acid Sequence Amino Acid Substitution Amino acids Animals Binding Sites Biological Sciences Ciona intestinalis Ciona intestinalis - enzymology Depolarization Electric current Electric potential Glycine - metabolism Inositols Ion Channel Gating Ion channels Ion Channels - metabolism Kinases Lipids Molecular Sequence Data Mutant Proteins - metabolism Mutation Oocytes Phosphatases Phosphates Phosphatidylinositol 4,5-Diphosphate - metabolism Phosphatidylinositols Phosphoric Monoester Hydrolases - chemistry Phosphoric Monoester Hydrolases - metabolism Phosphorylation PTEN Phosphohydrolase - chemistry Sequence Homology, Amino Acid Substrate Specificity Xenopus |
| title | voltage-sensing phosphatase, Ci-VSP, which shares sequence identity with PTEN, dephosphorylates phosphatidylinositol 4,5-bisphosphate |
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