Comparison of VILIP-1 and VILIP-3 binding to phospholipid monolayers.
Identifieur interne : 003716 ( PubMed/Curation ); précédent : 003715; suivant : 003717Comparison of VILIP-1 and VILIP-3 binding to phospholipid monolayers.
Auteurs : Samuel Rebaud [France] ; Anne Simon [France] ; Conan K. Wang [Australie] ; Lyndel Mason [Australie] ; Loïc Blum [France] ; Andreas Hofmann [Australie] ; Agnès Girard-Egrot [France]Source :
- PloS one [ 1932-6203 ] ; 2014.
Descripteurs français
- KwdFr :
- MESH :
- métabolisme : Calcium, Escherichia coli, Membrane cellulaire, Neurocalcine, Phospholipides.
- Liaison aux protéines.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Calcium, Neurocalcin, Phospholipids.
- metabolism : Cell Membrane, Escherichia coli.
- Protein Binding.
Abstract
The neuronal calcium sensor proteins Visinin-like Proteins 1 (VILIP-1) and 3 (VILIP-3) are effectors of guanylyl cyclase and acetyl choline receptors, and transduce calcium signals in the brain. The "calcium-myristoyl" switch, which involves a post-translationally added myristoyl moiety and calcium binding, is thought to regulate their membrane binding capacity and therefore, play a critical role in their mechanism of action. In the present study, we investigated the effect of membrane composition and solvent conditions on the membrane binding mechanisms of both VILIPs using lipid monolayers at the air/buffer interface. Results based on comparison of the adsorption kinetics of the myristoylated and non-myristoylated proteins confirm the pivotal role of calcium and the exposed myristol moiety for sustaining the membrane-bound state of both VILIPs. However, we also observed binding of both VILIP proteins in the absence of calcium and/or myristoyl conjugation. We propose a two-stage membrane binding mechanism for VILIP-1 and VILIP-3 whereby the proteins are initially attracted to the membrane surface by electrostatic interactions and possibly by specific interactions with highly negatively charged lipids head groups. The extrusion of the conjugated myristoyl group, and the subsequent anchoring in the membrane constitutes the second stage of the binding mechanism, and ensures the sustained membrane-bound form of these proteins.
DOI: 10.1371/journal.pone.0093948
PubMed: 24699524
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Curien, 43 bd du 11 Nov. 1918, F-69622 Villeurbanne cedex, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Institut de Chimie et Biochimie Moléculaires et Supramoléculaires, Université Lyon 1, University of Lyon, ICBMS, CNRS UMR 5246, Bât. Curien, 43 bd du 11 Nov. 1918, F-69622 Villeurbanne cedex</wicri:regionArea></affiliation></author><author><name sortKey="Simon, Anne" sort="Simon, Anne" uniqKey="Simon A" first="Anne" last="Simon">Anne Simon</name><affiliation wicri:level="1"><nlm:affiliation>Institut de Chimie et Biochimie Moléculaires et Supramoléculaires, Université Lyon 1, University of Lyon, ICBMS, CNRS UMR 5246, Bât. Curien, 43 bd du 11 Nov. 1918, F-69622 Villeurbanne cedex, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Institut de Chimie et Biochimie Moléculaires et Supramoléculaires, Université Lyon 1, University of Lyon, ICBMS, CNRS UMR 5246, Bât. Curien, 43 bd du 11 Nov. 1918, F-69622 Villeurbanne cedex</wicri:regionArea></affiliation></author><author><name sortKey="Wang, Conan K" sort="Wang, Conan K" uniqKey="Wang C" first="Conan K" last="Wang">Conan K. Wang</name><affiliation wicri:level="1"><nlm:affiliation>Structural Chemistry Program, Eskitis Institute, Griffith University, Brisbane, Queensland, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Structural Chemistry Program, Eskitis Institute, Griffith University, Brisbane, Queensland</wicri:regionArea></affiliation></author><author><name sortKey="Mason, Lyndel" sort="Mason, Lyndel" uniqKey="Mason L" first="Lyndel" last="Mason">Lyndel Mason</name><affiliation wicri:level="1"><nlm:affiliation>Structural Chemistry Program, Eskitis Institute, Griffith University, Brisbane, Queensland, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Structural Chemistry Program, Eskitis Institute, Griffith University, Brisbane, Queensland</wicri:regionArea></affiliation></author><author><name sortKey="Blum, Loic" sort="Blum, Loic" uniqKey="Blum L" first="Loïc" last="Blum">Loïc Blum</name><affiliation wicri:level="1"><nlm:affiliation>Institut de Chimie et Biochimie Moléculaires et Supramoléculaires, Université Lyon 1, University of Lyon, ICBMS, CNRS UMR 5246, Bât. Curien, 43 bd du 11 Nov. 1918, F-69622 Villeurbanne cedex, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Institut de Chimie et Biochimie Moléculaires et Supramoléculaires, Université Lyon 1, University of Lyon, ICBMS, CNRS UMR 5246, Bât. Curien, 43 bd du 11 Nov. 1918, F-69622 Villeurbanne cedex</wicri:regionArea></affiliation></author><author><name sortKey="Hofmann, Andreas" sort="Hofmann, Andreas" uniqKey="Hofmann A" first="Andreas" last="Hofmann">Andreas Hofmann</name><affiliation wicri:level="1"><nlm:affiliation>Structural Chemistry Program, Eskitis Institute, Griffith University, Brisbane, Queensland, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Structural Chemistry Program, Eskitis Institute, Griffith University, Brisbane, Queensland</wicri:regionArea></affiliation></author><author><name sortKey="Girard Egrot, Agnes" sort="Girard Egrot, Agnes" uniqKey="Girard Egrot A" first="Agnès" last="Girard-Egrot">Agnès Girard-Egrot</name><affiliation wicri:level="1"><nlm:affiliation>Institut de Chimie et Biochimie Moléculaires et Supramoléculaires, Université Lyon 1, University of Lyon, ICBMS, CNRS UMR 5246, Bât. Curien, 43 bd du 11 Nov. 1918, F-69622 Villeurbanne cedex, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Institut de Chimie et Biochimie Moléculaires et Supramoléculaires, Université Lyon 1, University of Lyon, ICBMS, CNRS UMR 5246, Bât. Curien, 43 bd du 11 Nov. 1918, F-69622 Villeurbanne cedex</wicri:regionArea></affiliation></author></analytic><series><title level="j">PloS one</title><idno type="eISSN">1932-6203</idno><imprint><date when="2014" type="published">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Calcium (metabolism)</term><term>Cell Membrane (metabolism)</term><term>Escherichia coli (metabolism)</term><term>Neurocalcin (metabolism)</term><term>Phospholipids (metabolism)</term><term>Protein Binding</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Calcium (métabolisme)</term><term>Escherichia coli (métabolisme)</term><term>Liaison aux protéines</term><term>Membrane cellulaire (métabolisme)</term><term>Neurocalcine (métabolisme)</term><term>Phospholipides (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Calcium</term><term>Neurocalcin</term><term>Phospholipids</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Cell Membrane</term><term>Escherichia coli</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Calcium</term><term>Escherichia coli</term><term>Membrane cellulaire</term><term>Neurocalcine</term><term>Phospholipides</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Protein Binding</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Liaison aux protéines</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The neuronal calcium sensor proteins Visinin-like Proteins 1 (VILIP-1) and 3 (VILIP-3) are effectors of guanylyl cyclase and acetyl choline receptors, and transduce calcium signals in the brain. The "calcium-myristoyl" switch, which involves a post-translationally added myristoyl moiety and calcium binding, is thought to regulate their membrane binding capacity and therefore, play a critical role in their mechanism of action. In the present study, we investigated the effect of membrane composition and solvent conditions on the membrane binding mechanisms of both VILIPs using lipid monolayers at the air/buffer interface. Results based on comparison of the adsorption kinetics of the myristoylated and non-myristoylated proteins confirm the pivotal role of calcium and the exposed myristol moiety for sustaining the membrane-bound state of both VILIPs. However, we also observed binding of both VILIP proteins in the absence of calcium and/or myristoyl conjugation. We propose a two-stage membrane binding mechanism for VILIP-1 and VILIP-3 whereby the proteins are initially attracted to the membrane surface by electrostatic interactions and possibly by specific interactions with highly negatively charged lipids head groups. The extrusion of the conjugated myristoyl group, and the subsequent anchoring in the membrane constitutes the second stage of the binding mechanism, and ensures the sustained membrane-bound form of these proteins.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">24699524</PMID><DateCreated><Year>2014</Year><Month>04</Month><Day>04</Day></DateCreated><DateCompleted><Year>2015</Year><Month>01</Month><Day>29</Day></DateCompleted><DateRevised><Year>2017</Year><Month>02</Month><Day>20</Day></DateRevised><Article PubModel="Electronic-eCollection"><Journal><ISSN IssnType="Electronic">1932-6203</ISSN><JournalIssue CitedMedium="Internet"><Volume>9</Volume><Issue>4</Issue><PubDate><Year>2014</Year></PubDate></JournalIssue><Title>PloS one</Title><ISOAbbreviation>PLoS ONE</ISOAbbreviation></Journal><ArticleTitle>Comparison of VILIP-1 and VILIP-3 binding to phospholipid monolayers.</ArticleTitle><Pagination><MedlinePgn>e93948</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1371/journal.pone.0093948</ELocationID><Abstract><AbstractText>The neuronal calcium sensor proteins Visinin-like Proteins 1 (VILIP-1) and 3 (VILIP-3) are effectors of guanylyl cyclase and acetyl choline receptors, and transduce calcium signals in the brain. The "calcium-myristoyl" switch, which involves a post-translationally added myristoyl moiety and calcium binding, is thought to regulate their membrane binding capacity and therefore, play a critical role in their mechanism of action. In the present study, we investigated the effect of membrane composition and solvent conditions on the membrane binding mechanisms of both VILIPs using lipid monolayers at the air/buffer interface. Results based on comparison of the adsorption kinetics of the myristoylated and non-myristoylated proteins confirm the pivotal role of calcium and the exposed myristol moiety for sustaining the membrane-bound state of both VILIPs. However, we also observed binding of both VILIP proteins in the absence of calcium and/or myristoyl conjugation. We propose a two-stage membrane binding mechanism for VILIP-1 and VILIP-3 whereby the proteins are initially attracted to the membrane surface by electrostatic interactions and possibly by specific interactions with highly negatively charged lipids head groups. The extrusion of the conjugated myristoyl group, and the subsequent anchoring in the membrane constitutes the second stage of the binding mechanism, and ensures the sustained membrane-bound form of these proteins.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Rebaud</LastName><ForeName>Samuel</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Institut de Chimie et Biochimie Moléculaires et Supramoléculaires, Université Lyon 1, University of Lyon, ICBMS, CNRS UMR 5246, Bât. Curien, 43 bd du 11 Nov. 1918, F-69622 Villeurbanne cedex, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Simon</LastName><ForeName>Anne</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Institut de Chimie et Biochimie Moléculaires et Supramoléculaires, Université Lyon 1, University of Lyon, ICBMS, CNRS UMR 5246, Bât. Curien, 43 bd du 11 Nov. 1918, F-69622 Villeurbanne cedex, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wang</LastName><ForeName>Conan K</ForeName><Initials>CK</Initials><AffiliationInfo><Affiliation>Structural Chemistry Program, Eskitis Institute, Griffith University, Brisbane, Queensland, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Mason</LastName><ForeName>Lyndel</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>Structural Chemistry Program, Eskitis Institute, Griffith University, Brisbane, Queensland, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Blum</LastName><ForeName>Loïc</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>Institut de Chimie et Biochimie Moléculaires et Supramoléculaires, Université Lyon 1, University of Lyon, ICBMS, CNRS UMR 5246, Bât. Curien, 43 bd du 11 Nov. 1918, F-69622 Villeurbanne cedex, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Hofmann</LastName><ForeName>Andreas</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Structural Chemistry Program, Eskitis Institute, Griffith University, Brisbane, Queensland, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Girard-Egrot</LastName><ForeName>Agnès</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Institut de Chimie et Biochimie Moléculaires et Supramoléculaires, Université Lyon 1, University of Lyon, ICBMS, CNRS UMR 5246, Bât. Curien, 43 bd du 11 Nov. 1918, F-69622 Villeurbanne cedex, France.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D003160">Comparative Study</PublicationType><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2014</Year><Month>04</Month><Day>03</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>PLoS One</MedlineTA><NlmUniqueID>101285081</NlmUniqueID><ISSNLinking>1932-6203</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C520235">HPCAL1 protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D051596">Neurocalcin</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance 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Version="1">7806504</PMID></CommentsCorrections></CommentsCorrectionsList><MeshHeadingList><MeshHeading><DescriptorName UI="D002118" MajorTopicYN="N">Calcium</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002462" MajorTopicYN="N">Cell Membrane</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004926" MajorTopicYN="N">Escherichia coli</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D051596" MajorTopicYN="N">Neurocalcin</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010743" MajorTopicYN="N">Phospholipids</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading></MeshHeadingList><OtherID Source="NLM">PMC3974848</OtherID></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2013</Year><Month>10</Month><Day>05</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2014</Year><Month>03</Month><Day>11</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2014</Year><Month>4</Month><Day>5</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2014</Year><Month>4</Month><Day>5</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2015</Year><Month>1</Month><Day>30</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>epublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">24699524</ArticleId><ArticleId IdType="doi">10.1371/journal.pone.0093948</ArticleId><ArticleId IdType="pii">PONE-D-13-40777</ArticleId><ArticleId 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