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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Regulation of P2X2 Receptors by the Neuronal Calcium Sensor VILIP1</title><author><name sortKey="Chaumont, Severine" sort="Chaumont, Severine" uniqKey="Chaumont S" first="Severine" last="Chaumont">Severine Chaumont</name><affiliation><nlm:aff id="A1">Department of Physiology, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, CA 90095, USA</nlm:aff></affiliation><affiliation><nlm:aff id="A2">Department of Neurobiology, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, CA 90095, USA</nlm:aff></affiliation><affiliation><nlm:aff id="A3">CNRS, UMR 5203, Institut de Génomique fonctionnelle, Montpellier, France</nlm:aff></affiliation><affiliation><nlm:aff id="A4">INSERM, U661, Montpellier, France</nlm:aff></affiliation><affiliation><nlm:aff id="A5">Université Montpellier, 1 and 2, 34094 Montpellier, France</nlm:aff></affiliation></author><author><name sortKey="Compan, Vincent" sort="Compan, Vincent" uniqKey="Compan V" first="Vincent" last="Compan">Vincent Compan</name><affiliation><nlm:aff id="A3">CNRS, UMR 5203, Institut de Génomique fonctionnelle, Montpellier, France</nlm:aff></affiliation><affiliation><nlm:aff id="A4">INSERM, U661, Montpellier, France</nlm:aff></affiliation><affiliation><nlm:aff id="A5">Université Montpellier, 1 and 2, 34094 Montpellier, France</nlm:aff></affiliation></author><author><name sortKey="Toulme, Estelle" sort="Toulme, Estelle" uniqKey="Toulme E" first="Estelle" last="Toulme">Estelle Toulme</name><affiliation><nlm:aff id="A1">Department of Physiology, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, CA 90095, USA</nlm:aff></affiliation><affiliation><nlm:aff id="A2">Department of Neurobiology, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, CA 90095, USA</nlm:aff></affiliation></author><author><name sortKey="Richler, Esther" sort="Richler, Esther" uniqKey="Richler E" first="Esther" last="Richler">Esther Richler</name><affiliation><nlm:aff id="A1">Department of Physiology, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, CA 90095, USA</nlm:aff></affiliation><affiliation><nlm:aff id="A2">Department of Neurobiology, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, CA 90095, USA</nlm:aff></affiliation></author><author><name sortKey="Housley, Gary D" sort="Housley, Gary D" uniqKey="Housley G" first="Gary D." last="Housley">Gary D. Housley</name><affiliation><nlm:aff id="A6">Department of Physiology, School of Medical Sciences, University of New South Wales, Sydney, New South Wales, NSW 2052 Australia</nlm:aff></affiliation></author><author><name sortKey="Rassendren, Francois" sort="Rassendren, Francois" uniqKey="Rassendren F" first="Francois" last="Rassendren">Francois Rassendren</name><affiliation><nlm:aff id="A3">CNRS, UMR 5203, Institut de Génomique fonctionnelle, Montpellier, France</nlm:aff></affiliation><affiliation><nlm:aff id="A4">INSERM, U661, Montpellier, France</nlm:aff></affiliation><affiliation><nlm:aff id="A5">Université Montpellier, 1 and 2, 34094 Montpellier, France</nlm:aff></affiliation></author><author><name sortKey="Khakh, Baljit S" sort="Khakh, Baljit S" uniqKey="Khakh B" first="Baljit S." last="Khakh">Baljit S. Khakh</name><affiliation><nlm:aff id="A1">Department of Physiology, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, CA 90095, USA</nlm:aff></affiliation><affiliation><nlm:aff id="A2">Department of Neurobiology, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, CA 90095, USA</nlm:aff></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">18922787</idno><idno type="pmc">3523710</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3523710</idno><idno type="RBID">PMC:3523710</idno><idno type="doi">10.1126/scisignal.1162329</idno><date when="2008">2008</date><idno type="wicri:Area/Pmc/Corpus">001E51</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">001E51</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Regulation of P2X2 Receptors by the Neuronal Calcium Sensor VILIP1</title><author><name sortKey="Chaumont, Severine" sort="Chaumont, Severine" uniqKey="Chaumont S" first="Severine" last="Chaumont">Severine Chaumont</name><affiliation><nlm:aff id="A1">Department of Physiology, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, CA 90095, USA</nlm:aff></affiliation><affiliation><nlm:aff id="A2">Department of Neurobiology, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, CA 90095, USA</nlm:aff></affiliation><affiliation><nlm:aff id="A3">CNRS, UMR 5203, Institut de Génomique fonctionnelle, Montpellier, France</nlm:aff></affiliation><affiliation><nlm:aff id="A4">INSERM, U661, Montpellier, France</nlm:aff></affiliation><affiliation><nlm:aff id="A5">Université Montpellier, 1 and 2, 34094 Montpellier, France</nlm:aff></affiliation></author><author><name sortKey="Compan, Vincent" sort="Compan, Vincent" uniqKey="Compan V" first="Vincent" last="Compan">Vincent Compan</name><affiliation><nlm:aff id="A3">CNRS, UMR 5203, Institut de Génomique fonctionnelle, Montpellier, France</nlm:aff></affiliation><affiliation><nlm:aff id="A4">INSERM, U661, Montpellier, France</nlm:aff></affiliation><affiliation><nlm:aff id="A5">Université Montpellier, 1 and 2, 34094 Montpellier, France</nlm:aff></affiliation></author><author><name sortKey="Toulme, Estelle" sort="Toulme, Estelle" uniqKey="Toulme E" first="Estelle" last="Toulme">Estelle Toulme</name><affiliation><nlm:aff id="A1">Department of Physiology, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, CA 90095, USA</nlm:aff></affiliation><affiliation><nlm:aff id="A2">Department of Neurobiology, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, CA 90095, USA</nlm:aff></affiliation></author><author><name sortKey="Richler, Esther" sort="Richler, Esther" uniqKey="Richler E" first="Esther" last="Richler">Esther Richler</name><affiliation><nlm:aff id="A1">Department of Physiology, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, CA 90095, USA</nlm:aff></affiliation><affiliation><nlm:aff id="A2">Department of Neurobiology, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, CA 90095, USA</nlm:aff></affiliation></author><author><name sortKey="Housley, Gary D" sort="Housley, Gary D" uniqKey="Housley G" first="Gary D." last="Housley">Gary D. Housley</name><affiliation><nlm:aff id="A6">Department of Physiology, School of Medical Sciences, University of New South Wales, Sydney, New South Wales, NSW 2052 Australia</nlm:aff></affiliation></author><author><name sortKey="Rassendren, Francois" sort="Rassendren, Francois" uniqKey="Rassendren F" first="Francois" last="Rassendren">Francois Rassendren</name><affiliation><nlm:aff id="A3">CNRS, UMR 5203, Institut de Génomique fonctionnelle, Montpellier, France</nlm:aff></affiliation><affiliation><nlm:aff id="A4">INSERM, U661, Montpellier, France</nlm:aff></affiliation><affiliation><nlm:aff id="A5">Université Montpellier, 1 and 2, 34094 Montpellier, France</nlm:aff></affiliation></author><author><name sortKey="Khakh, Baljit S" sort="Khakh, Baljit S" uniqKey="Khakh B" first="Baljit S." last="Khakh">Baljit S. Khakh</name><affiliation><nlm:aff id="A1">Department of Physiology, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, CA 90095, USA</nlm:aff></affiliation><affiliation><nlm:aff id="A2">Department of Neurobiology, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, CA 90095, USA</nlm:aff></affiliation></author></analytic><series><title level="j">Science signaling</title><idno type="eISSN">1937-9145</idno><imprint><date when="2008">2008</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p id="P1">Extracellular adenosine triphosphate (ATP) activates P2X receptors, which are involved in diverse physiological functions. Using a proteomic approach, we identified the neuronal calcium sensor VILIP1 as interacting with P2X2 receptors. We found that VILIP1 forms a signaling complex in vitro and in vivo with P2X2 receptors and regulates P2X2 receptor sensitivity to ATP, peak response, surface expression, and diffusion. VILIP1 constitutively binds to P2X2 receptors and displays enhanced interactions in an activation- and calcium-dependent manner owing to exposure of its binding segment in P2X2 receptors. VILIP1-P2X2 interactions are also enhanced in hippocampal neurons during conditions of action potential firing known to trigger P2X2 receptor activation. Our data thus reveal a previously unrecognized function for the neuronal calcium sensor protein VILIP1 and a mechanism for regulation of ATP-dependent P2X receptor signaling by neuronal calcium sensors.</p></div></front></TEI><pmc article-type="research-article"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<pmc-dir>properties manuscript</pmc-dir>
<front><journal-meta><journal-id journal-id-type="nlm-journal-id">101465400</journal-id><journal-id journal-id-type="pubmed-jr-id">34171</journal-id><journal-id journal-id-type="nlm-ta">Sci Signal</journal-id><journal-id journal-id-type="iso-abbrev">Sci Signal</journal-id><journal-title-group><journal-title>Science signaling</journal-title></journal-title-group><issn pub-type="epub">1937-9145</issn></journal-meta><article-meta><article-id pub-id-type="pmid">18922787</article-id><article-id pub-id-type="pmc">3523710</article-id><article-id pub-id-type="doi">10.1126/scisignal.1162329</article-id><article-id pub-id-type="manuscript">NIHMS425036</article-id><article-categories><subj-group subj-group-type="heading"><subject>Article</subject></subj-group></article-categories><title-group><article-title>Regulation of P2X2 Receptors by the Neuronal Calcium Sensor VILIP1</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Chaumont</surname><given-names>Severine</given-names></name><xref ref-type="aff" rid="A1">1</xref><xref ref-type="aff" rid="A2">2</xref><xref ref-type="aff" rid="A3">3</xref><xref ref-type="aff" rid="A4">4</xref><xref ref-type="aff" rid="A5">5</xref><xref rid="FN3" ref-type="author-notes">*</xref></contrib><contrib contrib-type="author"><name><surname>Compan</surname><given-names>Vincent</given-names></name><xref ref-type="aff" rid="A3">3</xref><xref ref-type="aff" rid="A4">4</xref><xref ref-type="aff" rid="A5">5</xref></contrib><contrib contrib-type="author"><name><surname>Toulme</surname><given-names>Estelle</given-names></name><xref ref-type="aff" rid="A1">1</xref><xref ref-type="aff" rid="A2">2</xref></contrib><contrib contrib-type="author"><name><surname>Richler</surname><given-names>Esther</given-names></name><xref ref-type="aff" rid="A1">1</xref><xref ref-type="aff" rid="A2">2</xref></contrib><contrib contrib-type="author"><name><surname>Housley</surname><given-names>Gary D.</given-names></name><xref ref-type="aff" rid="A6">6</xref></contrib><contrib contrib-type="author"><name><surname>Rassendren</surname><given-names>Francois</given-names></name><xref ref-type="aff" rid="A3">3</xref><xref ref-type="aff" rid="A4">4</xref><xref ref-type="aff" rid="A5">5</xref></contrib><contrib contrib-type="author"><name><surname>Khakh</surname><given-names>Baljit S.</given-names></name><xref ref-type="aff" rid="A1">1</xref><xref ref-type="aff" rid="A2">2</xref><xref rid="FN1" ref-type="author-notes">†</xref><xref rid="FN3" ref-type="author-notes">*</xref></contrib></contrib-group><aff id="A1"><label>1</label>Department of Physiology, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, CA 90095, USA</aff><aff id="A2"><label>2</label>Department of Neurobiology, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, CA 90095, USA</aff><aff id="A3"><label>3</label>CNRS, UMR 5203, Institut de Génomique fonctionnelle, Montpellier, France</aff><aff id="A4"><label>4</label>INSERM, U661, Montpellier, France</aff><aff id="A5"><label>5</label>Université Montpellier, 1 and 2, 34094 Montpellier, France</aff><aff id="A6"><label>6</label>Department of Physiology, School of Medical Sciences, University of New South Wales, Sydney, New South Wales, NSW 2052 Australia</aff><author-notes><corresp id="FN1"><label>†</label>To whom correspondence should be addressed. <email>bkhakh@mednet.ucla.edu</email></corresp><corresp id="FN2">Please direct general, editorial, FRET, spectroscopy, and electrophysiology correspondence to B. Khakh, <email>bkhakh@mednet.ucla.edu</email>; mass spectrometry and biochemistry correspondence to F. Rassendren, <email>francois.rassendren@igh.cnrs.fr</email>; and immunocytochemistry correspondence to G. Housley, <email>g.housley@unsw.edu.au</email></corresp><fn id="FN3" fn-type="equal"><label>*</label><p>These authors contributed equally to experiments in this work.</p></fn></author-notes><pub-date pub-type="nihms-submitted"><day>30</day><month>11</month><year>2012</year></pub-date><pub-date pub-type="epub"><day>14</day><month>10</month><year>2008</year></pub-date><pub-date pub-type="pmc-release"><day>17</day><month>12</month><year>2012</year></pub-date><volume>1</volume><issue>41</issue><fpage>ra8</fpage><lpage>ra8</lpage><permissions><copyright-statement>Copyright 2008 by the American Association for the Advancement of Science; all rights reserved.</copyright-statement><copyright-year>2008</copyright-year></permissions><abstract><p id="P1">Extracellular adenosine triphosphate (ATP) activates P2X receptors, which are involved in diverse physiological functions. Using a proteomic approach, we identified the neuronal calcium sensor VILIP1 as interacting with P2X2 receptors. We found that VILIP1 forms a signaling complex in vitro and in vivo with P2X2 receptors and regulates P2X2 receptor sensitivity to ATP, peak response, surface expression, and diffusion. VILIP1 constitutively binds to P2X2 receptors and displays enhanced interactions in an activation- and calcium-dependent manner owing to exposure of its binding segment in P2X2 receptors. VILIP1-P2X2 interactions are also enhanced in hippocampal neurons during conditions of action potential firing known to trigger P2X2 receptor activation. Our data thus reveal a previously unrecognized function for the neuronal calcium sensor protein VILIP1 and a mechanism for regulation of ATP-dependent P2X receptor signaling by neuronal calcium sensors.</p></abstract></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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