Specific interaction to PIP2 increases the kinetic rate of membrane binding of VILIPs, a subfamily of Neuronal Calcium Sensors (NCS) proteins.
Identifieur interne : 003195 ( PubMed/Checkpoint ); précédent : 003194; suivant : 003196Specific interaction to PIP2 increases the kinetic rate of membrane binding of VILIPs, a subfamily of Neuronal Calcium Sensors (NCS) proteins.
Auteurs : Samuel Rebaud [France] ; Conan K. Wang [Australie] ; Joe Sarkis [France] ; Lyndel Mason [Australie] ; Anne Simon [France] ; Loïc J. Blum [France] ; Andreas Hofmann [Australie] ; Agnès P. Girard-Egrot [France]Source :
- Biochimica et biophysica acta [ 0006-3002 ] ; 2014.
Descripteurs français
- KwdFr :
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Calcium, Neurocalcin, Phosphatidylinositol Phosphates.
- chemical , metabolism : Calcium, Neurocalcin, Phosphatidylinositol Phosphates.
- chemistry : Cell Membrane.
- metabolism : Cell Membrane.
- Humans, Lipoylation, Membranes, Artificial.
Abstract
VIsinin-LIke Proteins (VILIPs) are a subfamily of the Neuronal Calcium Sensor (NCS) proteins, which possess both N-myristoylation and EF-hand motifs allowing for a putative 'calcium-myristoyl switch' regulation mechanism. It has previously been established that myristoyl conjugation increases the affinity of proteins for membranes, but, in many cases, a second feature such as a cluster of positively-charged residues is needed for stable membrane binding. The interaction of two members of this family, VILIP-1 and VILIP-3, with Langmuir monolayers as membrane models has been investigated in order to study the effects of both myristoylation and the highly basic region containing conserved poly-lysine residues on membrane association kinetics and binding properties. Results show that in the presence of calcium, N-myristoylation significantly increases the kinetic rate of VILIP adsorption to the membrane. Additionally, the proteins bind to negatively charged phospholipids independently of the conjugated myristate moiety. Besides the regulatory effect of calcium on the rate of binding presumably due to exposure of the myristoyl moiety ascribed to their putative 'calcium-myristoyl switch', VILIP-1 and -3 also engage specific interactions with biomimetic membranes containing phosphatidylinositol 4,5-bisphosphate (PIP2). The presence of PIP2 increases the membrane association rates of both VILIPs. Taken together, these results show the major kinetic role of N-myristoylation for membrane binding, and highlight the critical role of specific phosphoinositide interactions for membrane association of members of the VILIP family.
DOI: 10.1016/j.bbamem.2014.06.021
PubMed: 25019684
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Curien, 43 bd du 11 Nov. 1918, F-69622 Villeurbanne cedex</wicri:regionArea><wicri:noRegion>69622 Villeurbanne cedex</wicri:noRegion><wicri:noRegion>69622 Villeurbanne cedex</wicri:noRegion></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 for Cell and Molecular Therapies, Griffith University, Brisbane Qld 4111, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Structural Chemistry Program, Eskitis Institute for Cell and Molecular Therapies, Griffith University, Brisbane Qld 4111</wicri:regionArea><wicri:noRegion>Brisbane Qld 4111</wicri:noRegion></affiliation></author><author><name sortKey="Sarkis, Joe" sort="Sarkis, Joe" uniqKey="Sarkis J" first="Joe" last="Sarkis">Joe Sarkis</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><wicri:noRegion>69622 Villeurbanne cedex</wicri:noRegion><wicri:noRegion>69622 Villeurbanne cedex</wicri:noRegion></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 for Cell and Molecular Therapies, Griffith University, Brisbane Qld 4111, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Structural Chemistry Program, Eskitis Institute for Cell and Molecular Therapies, Griffith University, Brisbane Qld 4111</wicri:regionArea><wicri:noRegion>Brisbane Qld 4111</wicri:noRegion></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><wicri:noRegion>69622 Villeurbanne cedex</wicri:noRegion><wicri:noRegion>69622 Villeurbanne cedex</wicri:noRegion></affiliation></author><author><name sortKey="Blum, Loic J" sort="Blum, Loic J" uniqKey="Blum L" first="Loïc J" last="Blum">Loïc J. 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><wicri:noRegion>69622 Villeurbanne cedex</wicri:noRegion><wicri:noRegion>69622 Villeurbanne cedex</wicri:noRegion></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 for Cell and Molecular Therapies, Griffith University, Brisbane Qld 4111, Australia; Faculty of Veterinary Science, The University of Melbourne, Parkville, Victoria, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Structural Chemistry Program, Eskitis Institute for Cell and Molecular Therapies, Griffith University, Brisbane Qld 4111, Australia; Faculty of Veterinary Science, The University of Melbourne, Parkville, Victoria</wicri:regionArea><wicri:noRegion>Victoria</wicri:noRegion></affiliation></author><author><name sortKey="Girard Egrot, Agnes P" sort="Girard Egrot, Agnes P" uniqKey="Girard Egrot A" first="Agnès P" last="Girard-Egrot">Agnès P. 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. Electronic address: agnes.girard-egrot@univ-lyon1.fr.</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><wicri:noRegion>69622 Villeurbanne cedex</wicri:noRegion><wicri:noRegion>69622 Villeurbanne cedex</wicri:noRegion></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2014">2014</date><idno type="RBID">pubmed:25019684</idno><idno type="pmid">25019684</idno><idno type="doi">10.1016/j.bbamem.2014.06.021</idno><idno type="wicri:Area/PubMed/Corpus">003441</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">003441</idno><idno type="wicri:Area/PubMed/Curation">003328</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">003328</idno><idno type="wicri:Area/PubMed/Checkpoint">003328</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">003328</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Specific interaction to PIP2 increases the kinetic rate of membrane binding of VILIPs, a subfamily of Neuronal Calcium Sensors (NCS) proteins.</title><author><name sortKey="Rebaud, Samuel" sort="Rebaud, Samuel" uniqKey="Rebaud S" first="Samuel" last="Rebaud">Samuel Rebaud</name><affiliation wicri:level="3"><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><placeName><region type="region" nuts="2">Auvergne-Rhône-Alpes</region><region type="old region" nuts="2">Rhône-Alpes</region><settlement type="city">Villeurbanne</settlement></placeName></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 for Cell and Molecular Therapies, Griffith University, Brisbane Qld 4111, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Structural Chemistry Program, Eskitis Institute for Cell and Molecular Therapies, Griffith University, Brisbane Qld 4111</wicri:regionArea><wicri:noRegion>Brisbane Qld 4111</wicri:noRegion></affiliation></author><author><name sortKey="Sarkis, Joe" sort="Sarkis, Joe" uniqKey="Sarkis J" first="Joe" last="Sarkis">Joe Sarkis</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><wicri:noRegion>69622 Villeurbanne cedex</wicri:noRegion><wicri:noRegion>69622 Villeurbanne cedex</wicri:noRegion></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 for Cell and Molecular Therapies, Griffith University, Brisbane Qld 4111, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Structural Chemistry Program, Eskitis Institute for Cell and Molecular Therapies, Griffith University, Brisbane Qld 4111</wicri:regionArea><wicri:noRegion>Brisbane Qld 4111</wicri:noRegion></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><wicri:noRegion>69622 Villeurbanne cedex</wicri:noRegion><wicri:noRegion>69622 Villeurbanne cedex</wicri:noRegion></affiliation></author><author><name sortKey="Blum, Loic J" sort="Blum, Loic J" uniqKey="Blum L" first="Loïc J" last="Blum">Loïc J. 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><wicri:noRegion>69622 Villeurbanne cedex</wicri:noRegion><wicri:noRegion>69622 Villeurbanne cedex</wicri:noRegion></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 for Cell and Molecular Therapies, Griffith University, Brisbane Qld 4111, Australia; Faculty of Veterinary Science, The University of Melbourne, Parkville, Victoria, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Structural Chemistry Program, Eskitis Institute for Cell and Molecular Therapies, Griffith University, Brisbane Qld 4111, Australia; Faculty of Veterinary Science, The University of Melbourne, Parkville, Victoria</wicri:regionArea><wicri:noRegion>Victoria</wicri:noRegion></affiliation></author><author><name sortKey="Girard Egrot, Agnes P" sort="Girard Egrot, Agnes P" uniqKey="Girard Egrot A" first="Agnès P" last="Girard-Egrot">Agnès P. 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. Electronic address: agnes.girard-egrot@univ-lyon1.fr.</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><wicri:noRegion>69622 Villeurbanne cedex</wicri:noRegion><wicri:noRegion>69622 Villeurbanne cedex</wicri:noRegion></affiliation></author></analytic><series><title level="j">Biochimica et biophysica acta</title><idno type="ISSN">0006-3002</idno><imprint><date when="2014" type="published">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Calcium (chemistry)</term><term>Calcium (metabolism)</term><term>Cell Membrane (chemistry)</term><term>Cell Membrane (metabolism)</term><term>Humans</term><term>Lipoylation</term><term>Membranes, Artificial</term><term>Neurocalcin (chemistry)</term><term>Neurocalcin (metabolism)</term><term>Phosphatidylinositol Phosphates (chemistry)</term><term>Phosphatidylinositol Phosphates (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Calcium ()</term><term>Calcium (métabolisme)</term><term>Humains</term><term>Lipoylation</term><term>Membrane artificielle</term><term>Membrane cellulaire ()</term><term>Membrane cellulaire (métabolisme)</term><term>Neurocalcine ()</term><term>Neurocalcine (métabolisme)</term><term>Phosphates phosphatidylinositol ()</term><term>Phosphates phosphatidylinositol (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Calcium</term><term>Neurocalcin</term><term>Phosphatidylinositol Phosphates</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Calcium</term><term>Neurocalcin</term><term>Phosphatidylinositol Phosphates</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Cell Membrane</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Cell Membrane</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Calcium</term><term>Membrane cellulaire</term><term>Neurocalcine</term><term>Phosphates phosphatidylinositol</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Humans</term><term>Lipoylation</term><term>Membranes, Artificial</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Calcium</term><term>Humains</term><term>Lipoylation</term><term>Membrane artificielle</term><term>Membrane cellulaire</term><term>Neurocalcine</term><term>Phosphates phosphatidylinositol</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">VIsinin-LIke Proteins (VILIPs) are a subfamily of the Neuronal Calcium Sensor (NCS) proteins, which possess both N-myristoylation and EF-hand motifs allowing for a putative 'calcium-myristoyl switch' regulation mechanism. It has previously been established that myristoyl conjugation increases the affinity of proteins for membranes, but, in many cases, a second feature such as a cluster of positively-charged residues is needed for stable membrane binding. The interaction of two members of this family, VILIP-1 and VILIP-3, with Langmuir monolayers as membrane models has been investigated in order to study the effects of both myristoylation and the highly basic region containing conserved poly-lysine residues on membrane association kinetics and binding properties. Results show that in the presence of calcium, N-myristoylation significantly increases the kinetic rate of VILIP adsorption to the membrane. Additionally, the proteins bind to negatively charged phospholipids independently of the conjugated myristate moiety. Besides the regulatory effect of calcium on the rate of binding presumably due to exposure of the myristoyl moiety ascribed to their putative 'calcium-myristoyl switch', VILIP-1 and -3 also engage specific interactions with biomimetic membranes containing phosphatidylinositol 4,5-bisphosphate (PIP2). The presence of PIP2 increases the membrane association rates of both VILIPs. Taken together, these results show the major kinetic role of N-myristoylation for membrane binding, and highlight the critical role of specific phosphoinositide interactions for membrane association of members of the VILIP family.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">25019684</PMID><DateCreated><Year>2014</Year><Month>08</Month><Day>06</Day></DateCreated><DateCompleted><Year>2014</Year><Month>10</Month><Day>01</Day></DateCompleted><DateRevised><Year>2016</Year><Month>11</Month><Day>26</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0006-3002</ISSN><JournalIssue CitedMedium="Print"><Volume>1838</Volume><Issue>10</Issue><PubDate><Year>2014</Year><Month>Oct</Month></PubDate></JournalIssue><Title>Biochimica et biophysica acta</Title><ISOAbbreviation>Biochim. Biophys. Acta</ISOAbbreviation></Journal><ArticleTitle>Specific interaction to PIP2 increases the kinetic rate of membrane binding of VILIPs, a subfamily of Neuronal Calcium Sensors (NCS) proteins.</ArticleTitle><Pagination><MedlinePgn>2698-707</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.bbamem.2014.06.021</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S0005-2736(14)00244-2</ELocationID><Abstract><AbstractText>VIsinin-LIke Proteins (VILIPs) are a subfamily of the Neuronal Calcium Sensor (NCS) proteins, which possess both N-myristoylation and EF-hand motifs allowing for a putative 'calcium-myristoyl switch' regulation mechanism. It has previously been established that myristoyl conjugation increases the affinity of proteins for membranes, but, in many cases, a second feature such as a cluster of positively-charged residues is needed for stable membrane binding. The interaction of two members of this family, VILIP-1 and VILIP-3, with Langmuir monolayers as membrane models has been investigated in order to study the effects of both myristoylation and the highly basic region containing conserved poly-lysine residues on membrane association kinetics and binding properties. Results show that in the presence of calcium, N-myristoylation significantly increases the kinetic rate of VILIP adsorption to the membrane. Additionally, the proteins bind to negatively charged phospholipids independently of the conjugated myristate moiety. Besides the regulatory effect of calcium on the rate of binding presumably due to exposure of the myristoyl moiety ascribed to their putative 'calcium-myristoyl switch', VILIP-1 and -3 also engage specific interactions with biomimetic membranes containing phosphatidylinositol 4,5-bisphosphate (PIP2). The presence of PIP2 increases the membrane association rates of both VILIPs. Taken together, these results show the major kinetic role of N-myristoylation for membrane binding, and highlight the critical role of specific phosphoinositide interactions for membrane association of members of the VILIP family.</AbstractText><CopyrightInformation>Copyright © 2014 Elsevier B.V. All rights reserved.</CopyrightInformation></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>Wang</LastName><ForeName>Conan K</ForeName><Initials>CK</Initials><AffiliationInfo><Affiliation>Structural Chemistry Program, Eskitis Institute for Cell and Molecular Therapies, Griffith University, Brisbane Qld 4111, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Sarkis</LastName><ForeName>Joe</ForeName><Initials>J</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>Mason</LastName><ForeName>Lyndel</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>Structural Chemistry Program, Eskitis Institute for Cell and Molecular Therapies, Griffith University, Brisbane Qld 4111, Australia.</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>Blum</LastName><ForeName>Loïc J</ForeName><Initials>LJ</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 for Cell and Molecular Therapies, Griffith University, Brisbane Qld 4111, Australia; Faculty of Veterinary Science, The University of Melbourne, Parkville, Victoria, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Girard-Egrot</LastName><ForeName>Agnès P</ForeName><Initials>AP</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. Electronic address: agnes.girard-egrot@univ-lyon1.fr.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><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>07</Month><Day>11</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Biochim Biophys Acta</MedlineTA><NlmUniqueID>0217513</NlmUniqueID><ISSNLinking>0006-3002</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C520235">HPCAL1 protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D008567">Membranes, Artificial</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D051596">Neurocalcin</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D018129">Phosphatidylinositol Phosphates</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C496688">VSNL1 protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C060980">phosphatidylinositol 3,4-diphosphate</NameOfSubstance></Chemical><Chemical><RegistryNumber>SY7Q814VUP</RegistryNumber><NameOfSubstance UI="D002118">Calcium</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D002118" MajorTopicYN="N">Calcium</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002462" MajorTopicYN="N">Cell Membrane</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054878" MajorTopicYN="Y">Lipoylation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008567" MajorTopicYN="Y">Membranes, Artificial</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D051596" MajorTopicYN="N">Neurocalcin</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018129" MajorTopicYN="N">Phosphatidylinositol Phosphates</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Calcium–myristoyl switch</Keyword><Keyword MajorTopicYN="N">Langmuir monolayer</Keyword><Keyword MajorTopicYN="N">Neuronal Calcium Sensor (NCS) proteins</Keyword><Keyword MajorTopicYN="N">Phosphoinositides</Keyword><Keyword MajorTopicYN="N">Protein–lipid interactions</Keyword><Keyword MajorTopicYN="N">VIsinin-LIke Proteins (VILIPs)</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2014</Year><Month>01</Month><Day>08</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2014</Year><Month>06</Month><Day>25</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2014</Year><Month>06</Month><Day>26</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2014</Year><Month>7</Month><Day>15</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2014</Year><Month>7</Month><Day>16</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2014</Year><Month>10</Month><Day>2</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">25019684</ArticleId><ArticleId IdType="pii">S0005-2736(14)00244-2</ArticleId><ArticleId IdType="doi">10.1016/j.bbamem.2014.06.021</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Australie</li><li>France</li></country><region><li>Auvergne-Rhône-Alpes</li><li>Rhône-Alpes</li></region><settlement><li>Villeurbanne</li></settlement></list><tree><country name="France"><region name="Auvergne-Rhône-Alpes"><name sortKey="Rebaud, Samuel" sort="Rebaud, Samuel" uniqKey="Rebaud S" first="Samuel" last="Rebaud">Samuel Rebaud</name></region><name sortKey="Blum, Loic J" sort="Blum, Loic J" uniqKey="Blum L" first="Loïc J" last="Blum">Loïc J. Blum</name><name sortKey="Girard Egrot, Agnes P" sort="Girard Egrot, Agnes P" uniqKey="Girard Egrot A" first="Agnès P" last="Girard-Egrot">Agnès P. Girard-Egrot</name><name sortKey="Sarkis, Joe" sort="Sarkis, Joe" uniqKey="Sarkis J" first="Joe" last="Sarkis">Joe Sarkis</name><name sortKey="Simon, Anne" sort="Simon, Anne" uniqKey="Simon A" first="Anne" last="Simon">Anne Simon</name></country><country name="Australie"><noRegion><name sortKey="Wang, Conan K" sort="Wang, Conan K" uniqKey="Wang C" first="Conan K" last="Wang">Conan K. Wang</name></noRegion><name sortKey="Hofmann, Andreas" sort="Hofmann, Andreas" uniqKey="Hofmann A" first="Andreas" last="Hofmann">Andreas Hofmann</name><name sortKey="Mason, Lyndel" sort="Mason, Lyndel" uniqKey="Mason L" first="Lyndel" last="Mason">Lyndel Mason</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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