Drosophila no‐dependent guanylyl cyclase is finely regulated by sequential order of coincidental signaling
Identifieur interne : 001B10 ( Istex/Corpus ); précédent : 001B09; suivant : 001B11Drosophila no‐dependent guanylyl cyclase is finely regulated by sequential order of coincidental signaling
Auteurs : Lixing Zhang ; Sylvette Tinette ; Alain RobichonSource :
- Journal of Cellular Biochemistry [ 0730-2312 ] ; 2002.
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Abstract
We investigate the mechanism of regulation of Drosophila‐soluble guanylate cyclase. Multiple putative sites of phosphorylation for the major kinases are present on both subunits of the heterodimer. We show that NO activation after binding to the heme group, is specifically modulated by sequential phosphorylations. PKA increases the NO stimulation at optimum level when both subunits are phosphorylated. Phosphorylation by CK (casein kinase‐like) first, inhibits the PKA phosphorylation of the alpha subunit and limits the PKA upregulation of the cyclase activity. However, PKA phosphorylation first didn't prevent CK phosphorylation of the two subunits and the sequence PKA/CK induces higher level of NO activation than CK/PKA. These phosphorylations occur independently of NO binding and the direct inhibitory effect of calcium is observed for all the sCG forms. These data show that the sGC activity is regulated in a complex way, and the well‐known asymmetry of the two subunits appears to cause the reading of the sequence of regulatory signals. This qualifies sGC as molecular detector on which converge coincidental and/or sequential neuronal signals. Furthermore, due to the fact that NO induction is huge (more than 600‐fold obtained with the mammal counterpart), we might consider that any variation in kinases activation and/or calcium concentration in micro area of neuronal processes, provokes locally significant quantitative difference of cGMP synthesis in presence of diffusing NO. J. Cell. Biochem. 85: 392–402, 2002. © 2002 Wiley‐Liss, Inc.
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DOI: 10.1002/jcb.10146
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<record><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title xml:lang="en">Drosophila no‐dependent guanylyl cyclase is finely regulated by sequential order of coincidental signaling</title><author><name sortKey="Zhang, Lixing" sort="Zhang, Lixing" uniqKey="Zhang L" first="Lixing" last="Zhang">Lixing Zhang</name><affiliation><mods:affiliation>CNRS, Centre Européen des Sciences du Goût, 15, rue Hugues Picardet, DIJON 21000, France</mods:affiliation></affiliation></author><author><name sortKey="Tinette, Sylvette" sort="Tinette, Sylvette" uniqKey="Tinette S" first="Sylvette" last="Tinette">Sylvette Tinette</name><affiliation><mods:affiliation>CNRS, Centre Européen des Sciences du Goût, 15, rue Hugues Picardet, DIJON 21000, France</mods:affiliation></affiliation></author><author><name sortKey="Robichon, Alain" sort="Robichon, Alain" uniqKey="Robichon A" first="Alain" last="Robichon">Alain Robichon</name><affiliation><mods:affiliation>CNRS, Centre Européen des Sciences du Goût, 15, rue Hugues Picardet, DIJON 21000, France</mods:affiliation></affiliation><affiliation><mods:affiliation>CNRS, Centre Européen des Sciences du Goût, 15, rue Hugues Picardet, DIJON 21000, France, FREE 2049.</mods:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:0DCCC2AD052A1B857A92676B0CF450161964601D</idno><date when="2002" year="2002">2002</date><idno type="doi">10.1002/jcb.10146</idno><idno type="url">https://api.istex.fr/document/0DCCC2AD052A1B857A92676B0CF450161964601D/fulltext/pdf</idno><idno type="wicri:Area/Istex/Corpus">001B10</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">001B10</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a" type="main" xml:lang="en">Drosophila no‐dependent guanylyl cyclase is finely regulated by sequential order of coincidental signaling</title><author><name sortKey="Zhang, Lixing" sort="Zhang, Lixing" uniqKey="Zhang L" first="Lixing" last="Zhang">Lixing Zhang</name><affiliation><mods:affiliation>CNRS, Centre Européen des Sciences du Goût, 15, rue Hugues Picardet, DIJON 21000, France</mods:affiliation></affiliation></author><author><name sortKey="Tinette, Sylvette" sort="Tinette, Sylvette" uniqKey="Tinette S" first="Sylvette" last="Tinette">Sylvette Tinette</name><affiliation><mods:affiliation>CNRS, Centre Européen des Sciences du Goût, 15, rue Hugues Picardet, DIJON 21000, France</mods:affiliation></affiliation></author><author><name sortKey="Robichon, Alain" sort="Robichon, Alain" uniqKey="Robichon A" first="Alain" last="Robichon">Alain Robichon</name><affiliation><mods:affiliation>CNRS, Centre Européen des Sciences du Goût, 15, rue Hugues Picardet, DIJON 21000, France</mods:affiliation></affiliation><affiliation><mods:affiliation>CNRS, Centre Européen des Sciences du Goût, 15, rue Hugues Picardet, DIJON 21000, France, FREE 2049.</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Journal of Cellular Biochemistry</title><title level="j" type="abbrev">J. Cell. Biochem.</title><idno type="ISSN">0730-2312</idno><idno type="eISSN">1097-4644</idno><imprint><publisher>Wiley Subscription Services, Inc., A Wiley Company</publisher><pubPlace>New York</pubPlace><date type="published" when="2002">2002</date><biblScope unit="volume">85</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="392">392</biblScope><biblScope unit="page" to="402">402</biblScope></imprint><idno type="ISSN">0730-2312</idno></series><idno type="istex">0DCCC2AD052A1B857A92676B0CF450161964601D</idno><idno type="DOI">10.1002/jcb.10146</idno><idno type="ArticleID">JCB10146</idno></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0730-2312</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Drosophila</term><term>cGMP</term><term>coincidental signaling</term><term>cyclase</term><term>neurons</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">We investigate the mechanism of regulation of Drosophila‐soluble guanylate cyclase. Multiple putative sites of phosphorylation for the major kinases are present on both subunits of the heterodimer. We show that NO activation after binding to the heme group, is specifically modulated by sequential phosphorylations. PKA increases the NO stimulation at optimum level when both subunits are phosphorylated. Phosphorylation by CK (casein kinase‐like) first, inhibits the PKA phosphorylation of the alpha subunit and limits the PKA upregulation of the cyclase activity. However, PKA phosphorylation first didn't prevent CK phosphorylation of the two subunits and the sequence PKA/CK induces higher level of NO activation than CK/PKA. These phosphorylations occur independently of NO binding and the direct inhibitory effect of calcium is observed for all the sCG forms. These data show that the sGC activity is regulated in a complex way, and the well‐known asymmetry of the two subunits appears to cause the reading of the sequence of regulatory signals. This qualifies sGC as molecular detector on which converge coincidental and/or sequential neuronal signals. Furthermore, due to the fact that NO induction is huge (more than 600‐fold obtained with the mammal counterpart), we might consider that any variation in kinases activation and/or calcium concentration in micro area of neuronal processes, provokes locally significant quantitative difference of cGMP synthesis in presence of diffusing NO. J. Cell. Biochem. 85: 392–402, 2002. © 2002 Wiley‐Liss, Inc.</div></front></TEI><istex><corpusName>wiley</corpusName><author><json:item><name>Lixing Zhang</name><affiliations><json:string>CNRS, Centre Européen des Sciences du Goût, 15, rue Hugues Picardet, DIJON 21000, France</json:string></affiliations></json:item><json:item><name>Sylvette Tinette</name><affiliations><json:string>CNRS, Centre Européen des Sciences du Goût, 15, rue Hugues Picardet, DIJON 21000, France</json:string></affiliations></json:item><json:item><name>Alain Robichon</name><affiliations><json:string>CNRS, Centre Européen des Sciences du Goût, 15, rue Hugues Picardet, DIJON 21000, France</json:string><json:string>CNRS, Centre Européen des Sciences du Goût, 15, rue Hugues Picardet, DIJON 21000, France, FREE 2049.</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>Drosophila</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>neurons</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>cyclase</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>cGMP</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>coincidental signaling</value></json:item></subject><articleId><json:string>JCB10146</json:string></articleId><language><json:string>eng</json:string></language><originalGenre><json:string>article</json:string></originalGenre><abstract>We investigate the mechanism of regulation of Drosophila‐soluble guanylate cyclase. Multiple putative sites of phosphorylation for the major kinases are present on both subunits of the heterodimer. We show that NO activation after binding to the heme group, is specifically modulated by sequential phosphorylations. PKA increases the NO stimulation at optimum level when both subunits are phosphorylated. Phosphorylation by CK (casein kinase‐like) first, inhibits the PKA phosphorylation of the alpha subunit and limits the PKA upregulation of the cyclase activity. However, PKA phosphorylation first didn't prevent CK phosphorylation of the two subunits and the sequence PKA/CK induces higher level of NO activation than CK/PKA. These phosphorylations occur independently of NO binding and the direct inhibitory effect of calcium is observed for all the sCG forms. These data show that the sGC activity is regulated in a complex way, and the well‐known asymmetry of the two subunits appears to cause the reading of the sequence of regulatory signals. This qualifies sGC as molecular detector on which converge coincidental and/or sequential neuronal signals. Furthermore, due to the fact that NO induction is huge (more than 600‐fold obtained with the mammal counterpart), we might consider that any variation in kinases activation and/or calcium concentration in micro area of neuronal processes, provokes locally significant quantitative difference of cGMP synthesis in presence of diffusing NO. J. Cell. 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biology</json:string></scienceMetrix></categories><publicationDate>2002</publicationDate><copyrightDate>2002</copyrightDate><doi><json:string>10.1002/jcb.10146</json:string></doi><id>0DCCC2AD052A1B857A92676B0CF450161964601D</id><score>0.19845274</score><fulltext><json:item><extension>pdf</extension><original>true</original><mimetype>application/pdf</mimetype><uri>https://api.istex.fr/document/0DCCC2AD052A1B857A92676B0CF450161964601D/fulltext/pdf</uri></json:item><json:item><extension>zip</extension><original>false</original><mimetype>application/zip</mimetype><uri>https://api.istex.fr/document/0DCCC2AD052A1B857A92676B0CF450161964601D/fulltext/zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/document/0DCCC2AD052A1B857A92676B0CF450161964601D/fulltext/tei"><teiHeader><fileDesc><titleStmt><title level="a" type="main" xml:lang="en">Drosophila no‐dependent guanylyl cyclase is finely regulated by sequential order of coincidental signaling</title></titleStmt><publicationStmt><authority>ISTEX</authority><publisher>Wiley Subscription Services, Inc., A Wiley Company</publisher><pubPlace>New York</pubPlace><availability><p>Copyright © 2002 Wiley‐Liss, Inc.</p></availability><date>2002</date></publicationStmt><notesStmt><note>CNRS</note><note>FREE - No. 2049;</note><note>Local government of Burgundy</note></notesStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a" type="main" xml:lang="en">Drosophila no‐dependent guanylyl cyclase is finely regulated by sequential order of coincidental signaling</title><author xml:id="author-1"><persName><forename type="first">Lixing</forename><surname>Zhang</surname></persName><note type="biography">Lixing Zhang is a scholar at Southern Yangtze University Duxi 214036, China and is presently supported by the Burgundy local government post doctoral fellowship.</note><affiliation>Lixing Zhang is a scholar at Southern Yangtze University Duxi 214036, China and is presently supported by the Burgundy local government post doctoral fellowship.</affiliation><affiliation>CNRS, Centre Européen des Sciences du Goût, 15, rue Hugues Picardet, DIJON 21000, France</affiliation></author><author xml:id="author-2"><persName><forename type="first">Sylvette</forename><surname>Tinette</surname></persName><affiliation>CNRS, Centre Européen des Sciences du Goût, 15, rue Hugues Picardet, DIJON 21000, France</affiliation></author><author xml:id="author-3"><persName><forename type="first">Alain</forename><surname>Robichon</surname></persName><affiliation>CNRS, Centre Européen des Sciences du Goût, 15, rue Hugues Picardet, DIJON 21000, France</affiliation><affiliation>CNRS, Centre Européen des Sciences du Goût, 15, rue Hugues Picardet, DIJON 21000, France, FREE 2049.</affiliation></author></analytic><monogr><title level="j">Journal of Cellular Biochemistry</title><title level="j" type="abbrev">J. Cell. Biochem.</title><idno type="pISSN">0730-2312</idno><idno type="eISSN">1097-4644</idno><idno type="DOI">10.1002/(ISSN)1097-4644</idno><imprint><publisher>Wiley Subscription Services, Inc., A Wiley Company</publisher><pubPlace>New York</pubPlace><date type="published" when="2002"></date><biblScope unit="volume">85</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="392">392</biblScope><biblScope unit="page" to="402">402</biblScope></imprint></monogr><idno type="istex">0DCCC2AD052A1B857A92676B0CF450161964601D</idno><idno type="DOI">10.1002/jcb.10146</idno><idno type="ArticleID">JCB10146</idno></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>2002</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>We investigate the mechanism of regulation of Drosophila‐soluble guanylate cyclase. Multiple putative sites of phosphorylation for the major kinases are present on both subunits of the heterodimer. We show that NO activation after binding to the heme group, is specifically modulated by sequential phosphorylations. PKA increases the NO stimulation at optimum level when both subunits are phosphorylated. Phosphorylation by CK (casein kinase‐like) first, inhibits the PKA phosphorylation of the alpha subunit and limits the PKA upregulation of the cyclase activity. However, PKA phosphorylation first didn't prevent CK phosphorylation of the two subunits and the sequence PKA/CK induces higher level of NO activation than CK/PKA. These phosphorylations occur independently of NO binding and the direct inhibitory effect of calcium is observed for all the sCG forms. These data show that the sGC activity is regulated in a complex way, and the well‐known asymmetry of the two subunits appears to cause the reading of the sequence of regulatory signals. This qualifies sGC as molecular detector on which converge coincidental and/or sequential neuronal signals. Furthermore, due to the fact that NO induction is huge (more than 600‐fold obtained with the mammal counterpart), we might consider that any variation in kinases activation and/or calcium concentration in micro area of neuronal processes, provokes locally significant quantitative difference of cGMP synthesis in presence of diffusing NO. J. Cell. Biochem. 85: 392–402, 2002. © 2002 Wiley‐Liss, Inc.</p></abstract><textClass xml:lang="en"><keywords scheme="keyword"><list><head>keywords</head><item><term>Drosophila</term></item><item><term>neurons</term></item><item><term>cyclase</term></item><item><term>cGMP</term></item><item><term>coincidental signaling</term></item></list></keywords></textClass><textClass><keywords scheme="Journal Subject"><list><head>article-category</head><item><term>Article</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="2001-10-17">Received</change><change when="2002-01-22">Registration</change><change when="2002">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/document/0DCCC2AD052A1B857A92676B0CF450161964601D/fulltext/txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Wiley, elements deleted: body"><istex:xmlDeclaration>version="1.0" encoding="UTF-8" standalone="yes"</istex:xmlDeclaration><istex:document><component version="2.0" type="serialArticle" xml:lang="en"><header><publicationMeta level="product"><publisherInfo><publisherName>Wiley Subscription Services, Inc., A Wiley Company</publisherName><publisherLoc>New York</publisherLoc></publisherInfo><doi registered="yes">10.1002/(ISSN)1097-4644</doi><issn type="print">0730-2312</issn><issn type="electronic">1097-4644</issn><idGroup><id type="product" value="JCB"></id></idGroup><titleGroup><title type="main" xml:lang="en" sort="JOURNAL OF CELLULAR BIOCHEMISTRY">Journal of Cellular Biochemistry</title><title type="short">J. 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Biochem.</title></titleGroup></publicationMeta><publicationMeta level="part" position="20"><doi origin="wiley" registered="yes">10.1002/jcb.v85:2</doi><numberingGroup><numbering type="journalVolume" number="85">85</numbering><numbering type="journalIssue">2</numbering></numberingGroup><coverDate startDate="2002">2002</coverDate></publicationMeta><publicationMeta level="unit" type="article" position="16" status="forIssue"><doi origin="wiley" registered="yes">10.1002/jcb.10146</doi><idGroup><id type="unit" value="JCB10146"></id></idGroup><countGroup><count type="pageTotal" number="11"></count></countGroup><titleGroup><title type="articleCategory">Article</title><title type="tocHeading1">Articles</title></titleGroup><copyright ownership="publisher">Copyright © 2002 Wiley‐Liss, Inc.</copyright><eventGroup><event type="manuscriptReceived" date="2001-10-17"></event><event type="manuscriptAccepted" date="2002-01-22"></event><event type="firstOnline" date="2002-02-28"></event><event type="publishedOnlineFinalForm" date="2002-03-13"></event><event type="xmlConverted" agent="Converter:JWSART34_TO_WML3G version:2.3.2 mode:FullText source:FullText result:FullText" date="2010-03-06"></event><event type="xmlConverted" agent="Converter:WILEY_ML3G_TO_WILEY_ML3GV2 version:3.8.8" date="2014-01-29"></event><event type="xmlConverted" agent="Converter:WML3G_To_WML3G version:4.1.7 mode:FullText,remove_FC" date="2014-10-23"></event></eventGroup><numberingGroup><numbering type="pageFirst">392</numbering><numbering type="pageLast">402</numbering></numberingGroup><correspondenceTo>CNRS, Centre Européen des Sciences du Goût, 15, rue Hugues Picardet, DIJON 21000, France, FREE 2049.</correspondenceTo><linkGroup><link type="toTypesetVersion" href="file:JCB.JCB10146.pdf"></link></linkGroup></publicationMeta><contentMeta><countGroup><count type="figureTotal" number="6"></count><count type="tableTotal" number="1"></count><count type="referenceTotal" number="39"></count><count type="wordTotal" number="7023"></count></countGroup><titleGroup><title type="main" xml:lang="en"><i>Drosophila</i> no‐dependent guanylyl cyclase is finely regulated by sequential order of coincidental signaling</title><title type="short" xml:lang="en">Guanylyl Cyclase & Coincidental Signaling</title></titleGroup><creators><creator xml:id="au1" creatorRole="author" affiliationRef="#af1" noteRef="#fn1"><personName><givenNames>Lixing</givenNames><familyName>Zhang</familyName></personName></creator><creator xml:id="au2" creatorRole="author" affiliationRef="#af1"><personName><givenNames>Sylvette</givenNames><familyName>Tinette</familyName></personName></creator><creator xml:id="au3" creatorRole="author" affiliationRef="#af1" corresponding="yes"><personName><givenNames>Alain</givenNames><familyName>Robichon</familyName></personName><contactDetails><email>robichon@cesg.cnrs.fr</email></contactDetails></creator></creators><affiliationGroup><affiliation xml:id="af1" countryCode="FR" type="organization"><unparsedAffiliation>CNRS, Centre Européen des Sciences du Goût, 15, rue Hugues Picardet, DIJON 21000, France</unparsedAffiliation></affiliation></affiliationGroup><keywordGroup xml:lang="en" type="author"><keyword xml:id="kwd1"><i>Drosophila</i></keyword><keyword xml:id="kwd2">neurons</keyword><keyword xml:id="kwd3">cyclase</keyword><keyword xml:id="kwd4">cGMP</keyword><keyword xml:id="kwd5">coincidental signaling</keyword></keywordGroup><fundingInfo><fundingAgency>CNRS</fundingAgency></fundingInfo><fundingInfo><fundingAgency>FREE</fundingAgency><fundingNumber>2049</fundingNumber></fundingInfo><fundingInfo><fundingAgency>Local government of Burgundy</fundingAgency></fundingInfo><abstractGroup><abstract type="main" xml:lang="en"><title type="main">Abstract</title><p>We investigate the mechanism of regulation of <i>Drosophila</i>‐soluble guanylate cyclase. Multiple putative sites of phosphorylation for the major kinases are present on both subunits of the heterodimer. We show that NO activation after binding to the heme group, is specifically modulated by sequential phosphorylations. PKA increases the NO stimulation at optimum level when both subunits are phosphorylated. Phosphorylation by CK (casein kinase‐like) first, inhibits the PKA phosphorylation of the alpha subunit and limits the PKA upregulation of the cyclase activity. However, PKA phosphorylation first didn't prevent CK phosphorylation of the two subunits and the sequence PKA/CK induces higher level of NO activation than CK/PKA. These phosphorylations occur independently of NO binding and the direct inhibitory effect of calcium is observed for all the sCG forms. These data show that the sGC activity is regulated in a complex way, and the well‐known asymmetry of the two subunits appears to cause the reading of the sequence of regulatory signals. This qualifies sGC as molecular detector on which converge coincidental and/or sequential neuronal signals. Furthermore, due to the fact that NO induction is huge (more than 600‐fold obtained with the mammal counterpart), we might consider that any variation in kinases activation and/or calcium concentration in micro area of neuronal processes, provokes locally significant quantitative difference of cGMP synthesis in presence of diffusing NO. J. Cell. Biochem. 85: 392–402, 2002. © 2002 Wiley‐Liss, Inc.</p></abstract></abstractGroup></contentMeta><noteGroup><note xml:id="fn1"><label>*</label><p>Lixing Zhang is a scholar at Southern Yangtze University Duxi 214036, China and is presently supported by the Burgundy local government post doctoral fellowship.</p></note></noteGroup></header></component></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Drosophila no‐dependent guanylyl cyclase is finely regulated by sequential order of coincidental signaling</title></titleInfo><titleInfo type="abbreviated" lang="en"><title>Guanylyl Cyclase & Coincidental Signaling</title></titleInfo><titleInfo type="alternative" contentType="CDATA" lang="en"><title>Drosophila no‐dependent guanylyl cyclase is finely regulated by sequential order of coincidental signaling</title></titleInfo><name type="personal"><namePart type="given">Lixing</namePart><namePart type="family">Zhang</namePart><affiliation>CNRS, Centre Européen des Sciences du Goût, 15, rue Hugues Picardet, DIJON 21000, France</affiliation><description>Lixing Zhang is a scholar at Southern Yangtze University Duxi 214036, China and is presently supported by the Burgundy local government post doctoral fellowship.</description><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Sylvette</namePart><namePart type="family">Tinette</namePart><affiliation>CNRS, Centre Européen des Sciences du Goût, 15, rue Hugues Picardet, DIJON 21000, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Alain</namePart><namePart type="family">Robichon</namePart><affiliation>CNRS, Centre Européen des Sciences du Goût, 15, rue Hugues Picardet, DIJON 21000, France</affiliation><affiliation>CNRS, Centre Européen des Sciences du Goût, 15, rue Hugues Picardet, DIJON 21000, France, FREE 2049.</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="article" displayLabel="article"></genre><originInfo><publisher>Wiley Subscription Services, Inc., A Wiley Company</publisher><place><placeTerm type="text">New York</placeTerm></place><dateIssued encoding="w3cdtf">2002</dateIssued><dateCaptured encoding="w3cdtf">2001-10-17</dateCaptured><dateValid encoding="w3cdtf">2002-01-22</dateValid><copyrightDate encoding="w3cdtf">2002</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><physicalDescription><internetMediaType>text/html</internetMediaType><extent unit="figures">6</extent><extent unit="tables">1</extent><extent unit="references">39</extent><extent unit="words">7023</extent></physicalDescription><abstract lang="en">We investigate the mechanism of regulation of Drosophila‐soluble guanylate cyclase. Multiple putative sites of phosphorylation for the major kinases are present on both subunits of the heterodimer. We show that NO activation after binding to the heme group, is specifically modulated by sequential phosphorylations. PKA increases the NO stimulation at optimum level when both subunits are phosphorylated. Phosphorylation by CK (casein kinase‐like) first, inhibits the PKA phosphorylation of the alpha subunit and limits the PKA upregulation of the cyclase activity. However, PKA phosphorylation first didn't prevent CK phosphorylation of the two subunits and the sequence PKA/CK induces higher level of NO activation than CK/PKA. These phosphorylations occur independently of NO binding and the direct inhibitory effect of calcium is observed for all the sCG forms. These data show that the sGC activity is regulated in a complex way, and the well‐known asymmetry of the two subunits appears to cause the reading of the sequence of regulatory signals. This qualifies sGC as molecular detector on which converge coincidental and/or sequential neuronal signals. Furthermore, due to the fact that NO induction is huge (more than 600‐fold obtained with the mammal counterpart), we might consider that any variation in kinases activation and/or calcium concentration in micro area of neuronal processes, provokes locally significant quantitative difference of cGMP synthesis in presence of diffusing NO. J. Cell. Biochem. 85: 392–402, 2002. © 2002 Wiley‐Liss, Inc.</abstract><note type="funding">CNRS</note><note type="funding">FREE - No. 2049; </note><note type="funding">Local government of Burgundy</note><subject lang="en"><genre>keywords</genre><topic>Drosophila</topic><topic>neurons</topic><topic>cyclase</topic><topic>cGMP</topic><topic>coincidental signaling</topic></subject><relatedItem type="host"><titleInfo><title>Journal of Cellular Biochemistry</title></titleInfo><titleInfo type="abbreviated"><title>J. Cell. 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