Effect of Ser-129 Phosphorylation on Interaction of α-Synuclein with Synaptic and Cellular Membranes*
Identifieur interne : 000561 ( Pmc/Curation ); précédent : 000560; suivant : 000562Effect of Ser-129 Phosphorylation on Interaction of α-Synuclein with Synaptic and Cellular Membranes*
Auteurs : Naomi P. Visanji ; Sabine Wislet-Gendebien [Belgique] ; Loren W. Oschipok ; Gang Zhang ; Isabelle Aubert ; Paul E. Fraser ; Anurag Tandon [Canada]Source :
- The Journal of Biological Chemistry [ 0021-9258 ] ; 2011.
Abstract
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DOI: 10.1074/jbc.M111.253450
PubMed: 21849493
PubMed Central: 3195582
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Effect of Ser-129 Phosphorylation on Interaction of α-Synuclein with Synaptic and Cellular Membranes<xref ref-type="fn" rid="FN1">*</xref><xref ref-type="fn" rid="FN2"><sup><inline-graphic xlink:href="sbox.jpg"></inline-graphic></sup></xref></title><author><name sortKey="Visanji, Naomi P" sort="Visanji, Naomi P" uniqKey="Visanji N" first="Naomi P." last="Visanji">Naomi P. Visanji</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Wislet Gendebien, Sabine" sort="Wislet Gendebien, Sabine" uniqKey="Wislet Gendebien S" first="Sabine" last="Wislet-Gendebien">Sabine Wislet-Gendebien</name><affiliation wicri:level="1"><nlm:aff id="aff2">GIGA Neurosciences, University of Liege, 1 Avenue de l'Hôpital, 4000 Liège, Belgium,</nlm:aff><country xml:lang="fr">Belgique</country><wicri:regionArea>GIGA Neurosciences, University of Liege, 1 Avenue de l'Hôpital, 4000 Liège</wicri:regionArea></affiliation></author><author><name sortKey="Oschipok, Loren W" sort="Oschipok, Loren W" uniqKey="Oschipok L" first="Loren W." last="Oschipok">Loren W. Oschipok</name><affiliation><nlm:aff id="aff3"></nlm:aff></affiliation></author><author><name sortKey="Zhang, Gang" sort="Zhang, Gang" uniqKey="Zhang G" first="Gang" last="Zhang">Gang Zhang</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Aubert, Isabelle" sort="Aubert, Isabelle" uniqKey="Aubert I" first="Isabelle" last="Aubert">Isabelle Aubert</name><affiliation><nlm:aff id="aff4"></nlm:aff></affiliation></author><author><name sortKey="Fraser, Paul E" sort="Fraser, Paul E" uniqKey="Fraser P" first="Paul E." last="Fraser">Paul E. Fraser</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation><affiliation><nlm:aff id="aff5"></nlm:aff></affiliation></author><author><name sortKey="Tandon, Anurag" sort="Tandon, Anurag" uniqKey="Tandon A" first="Anurag" last="Tandon">Anurag Tandon</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation><affiliation wicri:level="1"><nlm:aff id="aff6">Medicine, University of Toronto, Toronto, Ontario M5S 1A8, Canada</nlm:aff><country xml:lang="fr">Canada</country><wicri:regionArea>Medicine, University of Toronto, Toronto, Ontario M5S 1A8</wicri:regionArea></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">21849493</idno><idno type="pmc">3195582</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3195582</idno><idno type="RBID">PMC:3195582</idno><idno type="doi">10.1074/jbc.M111.253450</idno><date when="2011">2011</date><idno type="wicri:Area/Pmc/Corpus">000561</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000561</idno><idno type="wicri:Area/Pmc/Curation">000561</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Curation">000561</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Effect of Ser-129 Phosphorylation on Interaction of α-Synuclein with Synaptic and Cellular Membranes<xref ref-type="fn" rid="FN1">*</xref><xref ref-type="fn" rid="FN2"><sup><inline-graphic xlink:href="sbox.jpg"></inline-graphic></sup></xref></title><author><name sortKey="Visanji, Naomi P" sort="Visanji, Naomi P" uniqKey="Visanji N" first="Naomi P." last="Visanji">Naomi P. Visanji</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Wislet Gendebien, Sabine" sort="Wislet Gendebien, Sabine" uniqKey="Wislet Gendebien S" first="Sabine" last="Wislet-Gendebien">Sabine Wislet-Gendebien</name><affiliation wicri:level="1"><nlm:aff id="aff2">GIGA Neurosciences, University of Liege, 1 Avenue de l'Hôpital, 4000 Liège, Belgium,</nlm:aff><country xml:lang="fr">Belgique</country><wicri:regionArea>GIGA Neurosciences, University of Liege, 1 Avenue de l'Hôpital, 4000 Liège</wicri:regionArea></affiliation></author><author><name sortKey="Oschipok, Loren W" sort="Oschipok, Loren W" uniqKey="Oschipok L" first="Loren W." last="Oschipok">Loren W. Oschipok</name><affiliation><nlm:aff id="aff3"></nlm:aff></affiliation></author><author><name sortKey="Zhang, Gang" sort="Zhang, Gang" uniqKey="Zhang G" first="Gang" last="Zhang">Gang Zhang</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Aubert, Isabelle" sort="Aubert, Isabelle" uniqKey="Aubert I" first="Isabelle" last="Aubert">Isabelle Aubert</name><affiliation><nlm:aff id="aff4"></nlm:aff></affiliation></author><author><name sortKey="Fraser, Paul E" sort="Fraser, Paul E" uniqKey="Fraser P" first="Paul E." last="Fraser">Paul E. Fraser</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation><affiliation><nlm:aff id="aff5"></nlm:aff></affiliation></author><author><name sortKey="Tandon, Anurag" sort="Tandon, Anurag" uniqKey="Tandon A" first="Anurag" last="Tandon">Anurag Tandon</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation><affiliation wicri:level="1"><nlm:aff id="aff6">Medicine, University of Toronto, Toronto, Ontario M5S 1A8, Canada</nlm:aff><country xml:lang="fr">Canada</country><wicri:regionArea>Medicine, University of Toronto, Toronto, Ontario M5S 1A8</wicri:regionArea></affiliation></author></analytic><series><title level="j">The Journal of Biological Chemistry</title><idno type="ISSN">0021-9258</idno><idno type="eISSN">1083-351X</idno><imprint><date when="2011">2011</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p><bold>Background:</bold> The majority of α-synuclein is phosphorylated at serine 129 in Lewy bodies.</p><p><bold>Results:</bold> The membrane association of PD-linked mutant α-synuclein, but not wild-type α-synuclein, was increased by serine 129 phosphorylation.</p><p><bold>Conclusion:</bold> Pathological serine 129 phosphorylation regulates membrane accumulation of mutant α-synuclein.</p><p><bold>Significance:</bold> The relationship of serine 129 phosphorylation to pathogenic aggregation of normal and mutant α-synuclein may be governed by distinct effects on phosphoprotein membrane accumulation.</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>
<front><journal-meta><journal-id journal-id-type="nlm-ta">J Biol Chem</journal-id><journal-id journal-id-type="hwp">jbc</journal-id><journal-id journal-id-type="pmc">jbc</journal-id><journal-id journal-id-type="publisher-id">JBC</journal-id><journal-title-group><journal-title>The Journal of Biological Chemistry</journal-title></journal-title-group><issn pub-type="ppub">0021-9258</issn><issn pub-type="epub">1083-351X</issn><publisher><publisher-name>American Society for Biochemistry and Molecular Biology</publisher-name><publisher-loc>9650 Rockville Pike, Bethesda, MD 20814, U.S.A.</publisher-loc></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">21849493</article-id><article-id pub-id-type="pmc">3195582</article-id><article-id pub-id-type="publisher-id">M111.253450</article-id><article-id pub-id-type="doi">10.1074/jbc.M111.253450</article-id><article-categories><subj-group subj-group-type="heading"><subject>Molecular Bases of Disease</subject></subj-group></article-categories><title-group><article-title>Effect of Ser-129 Phosphorylation on Interaction of α-Synuclein with Synaptic and Cellular Membranes<xref ref-type="fn" rid="FN1">*</xref><xref ref-type="fn" rid="FN2"><sup><inline-graphic xlink:href="sbox.jpg"></inline-graphic></sup></xref></article-title><alt-title alt-title-type="short">Ser-129 Phosphorylation and Membrane Binding of α-Synuclein</alt-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Visanji</surname><given-names>Naomi P.</given-names></name><xref ref-type="aff" rid="aff1"><sup>‡</sup></xref><xref ref-type="author-notes" rid="FN3"><sup>1</sup></xref><xref ref-type="author-notes" rid="FN4"><sup>2</sup></xref></contrib><contrib contrib-type="author"><name><surname>Wislet-Gendebien</surname><given-names>Sabine</given-names></name><xref ref-type="aff" rid="aff2"><sup>§</sup></xref><xref ref-type="author-notes" rid="FN3"><sup>1</sup></xref><xref ref-type="author-notes" rid="FN5"><sup>3</sup></xref></contrib><contrib contrib-type="author"><name><surname>Oschipok</surname><given-names>Loren W.</given-names></name><xref ref-type="aff" rid="aff3"><sup>¶</sup></xref></contrib><contrib contrib-type="author"><name><surname>Zhang</surname><given-names>Gang</given-names></name><xref ref-type="aff" rid="aff1"><sup>‡</sup></xref></contrib><contrib contrib-type="author"><name><surname>Aubert</surname><given-names>Isabelle</given-names></name><xref ref-type="aff" rid="aff4"><sup>‖</sup></xref></contrib><contrib contrib-type="author"><name><surname>Fraser</surname><given-names>Paul E.</given-names></name><xref ref-type="aff" rid="aff1"><sup>‡</sup></xref><xref ref-type="aff" rid="aff5">**</xref></contrib><contrib contrib-type="author"><name><surname>Tandon</surname><given-names>Anurag</given-names></name><xref ref-type="aff" rid="aff1"><sup>‡</sup></xref><xref ref-type="aff" rid="aff6"><sup>‡‡</sup></xref><xref ref-type="corresp" rid="cor1"><sup>4</sup></xref></contrib><aff id="aff1">From the<label>‡</label>Centre for Research in Neurodegenerative Diseases, University of Toronto, Toronto, Ontario M5S 3H2, Canada,</aff><aff id="aff2"><label>§</label>GIGA Neurosciences, University of Liege, 1 Avenue de l'Hôpital, 4000 Liège, Belgium,</aff><aff id="aff3">the<label>¶</label>Brain Research Centre, University of British Columbia, British Columbia V6T 2B5, Canada,</aff><aff id="aff4">the<label>‖</label>Sunnybrook Research Institute and Department of Laboratory Medicine and Pathobiology, University of Toronto, Toronto, Ontario M4N 3M5, Canada, and</aff><aff id="aff5">the Departments of<label>**</label>Medical Biophysics and</aff><aff id="aff6"><label>‡‡</label>Medicine, University of Toronto, Toronto, Ontario M5S 1A8, Canada</aff></contrib-group><author-notes><corresp id="cor1"><label>4</label> To whom correspondence should be addressed: <addr-line>Centre for Research in Neurodegenerative Diseases, University of Toronto, 6 Queen's Park Crescent West, Toronto, Ontario M5S 3H2, Canada.</addr-line> Tel.: <phone>416-978-8880</phone>; Fax: <fax>416-978-1878</fax>; E-mail: <email>a.tandon@utoronto.ca</email>.</corresp><fn fn-type="equal" id="FN3"><label>1</label><p>Both authors contributed equally to this work.</p></fn><fn fn-type="supported-by" id="FN4"><label>2</label><p>Supported by a fellowship from the Parkinson Society of Canada.</p></fn><fn fn-type="supported-by" id="FN5"><label>3</label><p>Supported by a fellowship from the Canadian Institutes of Health Research.</p></fn></author-notes><pub-date pub-type="ppub"><day>14</day><month>10</month><year>2011</year></pub-date><pub-date pub-type="epub"><day>17</day><month>8</month><year>2011</year></pub-date><volume>286</volume><issue>41</issue><fpage>35863</fpage><lpage>35873</lpage><history><date date-type="received"><day>20</day><month>4</month><year>2011</year></date><date date-type="rev-recd"><day>11</day><month>8</month><year>2011</year></date></history><permissions><copyright-statement>© 2011 by The American Society for Biochemistry and Molecular Biology, Inc.</copyright-statement><copyright-year>2011</copyright-year></permissions><self-uri xlink:title="pdf" xlink:type="simple" xlink:href="zbc04111035863.pdf"></self-uri><abstract abstract-type="teaser"><p><bold>Background:</bold> The majority of α-synuclein is phosphorylated at serine 129 in Lewy bodies.</p><p><bold>Results:</bold> The membrane association of PD-linked mutant α-synuclein, but not wild-type α-synuclein, was increased by serine 129 phosphorylation.</p><p><bold>Conclusion:</bold> Pathological serine 129 phosphorylation regulates membrane accumulation of mutant α-synuclein.</p><p><bold>Significance:</bold> The relationship of serine 129 phosphorylation to pathogenic aggregation of normal and mutant α-synuclein may be governed by distinct effects on phosphoprotein membrane accumulation.</p></abstract><abstract><p>In the healthy brain, less than 5% of α-synuclein (α-syn) is phosphorylated at serine 129 (Ser(P)-129). However, within Parkinson disease (PD) Lewy bodies, 89% of α-syn is Ser(P)-129. The effects of Ser(P)-129 modification on α-syn distribution and solubility are poorly understood. As α-syn normally exists in both membrane-bound and cytosolic compartments, we examined the binding and dissociation of Ser(P)-129 α-syn and analyzed the effects of manipulating Ser(P)-129 levels on α-syn membrane interactions using synaptosomal membranes and neural precursor cells from α-syn-deficient mice or transgenic mice expressing human α-syn. We first evaluated the recovery of the Ser(P)-129 epitope following either α-syn membrane binding or dissociation. We demonstrate a rapid turnover of Ser(P)-129 during both binding to and dissociation from synaptic membranes. Although the membrane binding of WT α-syn was insensitive to modulation of Ser(P)-129 levels by multiple strategies (the use of phosphomimic S129D and nonphosphorylated S129A α-syn mutants; by enzymatic dephosphorylation of Ser(P)-129 or proteasome inhibitor-induced elevation in Ser(P)-129; or by inhibition or stable overexpression of PLK2), PD mutant Ser(P)-129 α-syn showed a preferential membrane association compared with WT Ser(P)-129 α-syn. Collectively, these data suggest that phosphorylation at Ser-129 is dynamic and that the subcellular distribution of α-syn bearing PD-linked mutations, A30P or A53T, is influenced by the phosphorylation state of Ser-129.</p></abstract><kwd-group><kwd>Neurodegeneration</kwd><kwd>Parkinson Disease</kwd><kwd>Phosphatase</kwd><kwd>Post-translational Modification</kwd><kwd>Protein Phosphorylation</kwd><kwd>Subcellular Fractionation</kwd><kwd>Synuclein</kwd><kwd>Kinase</kwd><kwd>Membrane Binding</kwd><kwd>Synaptosome</kwd></kwd-group></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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