Differential regulation of wild-type and mutant alpha-synuclein binding to synaptic membranes by cytosolic factors
Identifieur interne : 002206 ( Main/Exploration ); précédent : 002205; suivant : 002207Differential regulation of wild-type and mutant alpha-synuclein binding to synaptic membranes by cytosolic factors
Auteurs : Sabine Wislet-Gendebien [Canada, Belgique] ; Naomi P. Visanji [Canada] ; Shawn N. Whitehead [Canada] ; Diana Marsilio [Canada] ; Weimin Hou [Canada] ; Daniel Figeys [Canada] ; Paul E. Fraser [Canada] ; Steffany Al Bennett [Canada] ; Anurag Tandon [Canada]Source :
- BMC Neuroscience [ 1471-2202 ] ; 2008.
English descriptors
- KwdEn :
- Adenosine Triphosphate (analysis), Adenosine Triphosphate (metabolism), Animals, Blotting, Western, Brain Chemistry, Calcium (analysis), Calcium (metabolism), Cytosol (chemistry), Cytosol (metabolism), Genotype, Humans, Lipids (analysis), Membrane Proteins (chemistry), Membrane Proteins (genetics), Membrane Proteins (metabolism), Mice, Mice, Knockout, Mutation, Mutation, Missense, Parkinson Disease (genetics), Parkinson Disease (metabolism), Platelet Activating Factor (analogs & derivatives), Platelet Activating Factor (analysis), Platelet Activating Factor (metabolism), Protein Binding, Synaptic Membranes (metabolism), Synaptosomes (metabolism), alpha-Synuclein (analysis), alpha-Synuclein (genetics), alpha-Synuclein (metabolism).
- MESH :
- chemical , analogs & derivatives : Platelet Activating Factor.
- chemical , analysis : Adenosine Triphosphate, Calcium, Lipids, Platelet Activating Factor, alpha-Synuclein.
- chemical , chemistry : Membrane Proteins.
- chemical , genetics : Membrane Proteins, alpha-Synuclein.
- chemical , metabolism : Adenosine Triphosphate, Calcium, Membrane Proteins, Platelet Activating Factor, alpha-Synuclein.
- chemistry : Cytosol.
- genetics : Parkinson Disease.
- metabolism : Cytosol, Parkinson Disease, Synaptic Membranes, Synaptosomes.
- Animals, Blotting, Western, Brain Chemistry, Genotype, Humans, Mice, Mice, Knockout, Mutation, Mutation, Missense, Protein Binding.
Abstract
Alpha-Synuclein (α-syn), a 140 amino acid protein associated with presynaptic membranes in brain, is a major constituent of Lewy bodies in Parkinson's disease (PD). Three missense mutations (A30P, A53T and E46K) in the α-syn gene are associated with rare autosomal dominant forms of familial PD. However, the regulation of α-syn's cellular localization in neurons and the effects of the PD-linked mutations are poorly understood.
In the present study, we analysed the ability of cytosolic factors to regulate α-syn binding to synaptic membranes. We show that co-incubation with brain cytosol significantly increases the membrane binding of normal and PD-linked mutant α-syn. To characterize cytosolic factor(s) that modulate α-syn binding properties, we investigated the ability of proteins, lipids, ATP and calcium to modulate α-syn membrane interactions. We report that lipids and ATP are two of the principal cytosolic components that modulate Wt and A53T α-syn binding to the synaptic membrane. We further show that 1-O-hexadecyl-2-acetyl-
These findings suggest that endogenous brain cytosolic factors regulate Wt and mutant α-syn membrane binding, and could represent potential targets to influence α-syn solubility in brain.
Url:
DOI: 10.1186/1471-2202-9-92
PubMed: 18808659
PubMed Central: 2562387
Affiliations:
- Belgique, Canada
- Ontario, Province de Liège
- Liège, Toronto
- Université de Liège, Université de Toronto
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Le document en format XML
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Fraser</name><affiliation wicri:level="4"><nlm:aff id="I1">Centre for Research in Neurodegenerative Diseases, University of Toronto, Toronto, Ontario, M5S 3H2 Canada</nlm:aff><orgName type="university">Université de Toronto</orgName><country>Canada</country><placeName><settlement type="city">Toronto</settlement><region type="state">Ontario</region></placeName></affiliation></author><author><name sortKey="Bennett, Steffany Al" sort="Bennett, Steffany Al" uniqKey="Bennett S" first="Steffany Al" last="Bennett">Steffany Al Bennett</name><affiliation wicri:level="1"><nlm:aff id="I3">Neural Regeneration Laboratory, Ottawa Institute of Systems Biology, Department of Biochemistry, Microbiology, and Immunology, University of Ottawa, Ottawa, K1H 8M5, Canada</nlm:aff><country xml:lang="fr">Canada</country><wicri:regionArea>Neural Regeneration Laboratory, Ottawa Institute of Systems Biology, Department of Biochemistry, Microbiology, and Immunology, University of Ottawa, Ottawa, K1H 8M5</wicri:regionArea><wicri:noRegion>K1H 8M5</wicri:noRegion></affiliation></author><author><name sortKey="Tandon, Anurag" sort="Tandon, Anurag" uniqKey="Tandon A" first="Anurag" last="Tandon">Anurag Tandon</name><affiliation wicri:level="4"><nlm:aff id="I1">Centre for Research in Neurodegenerative Diseases, University of Toronto, Toronto, Ontario, M5S 3H2 Canada</nlm:aff><orgName type="university">Université de Toronto</orgName><country>Canada</country><placeName><settlement type="city">Toronto</settlement><region type="state">Ontario</region></placeName></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">18808659</idno><idno type="pmc">2562387</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2562387</idno><idno type="RBID">PMC:2562387</idno><idno type="doi">10.1186/1471-2202-9-92</idno><date when="2008">2008</date><idno type="wicri:Area/Pmc/Corpus">000329</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000329</idno><idno type="wicri:Area/Pmc/Curation">000329</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Curation">000329</idno><idno type="wicri:Area/Pmc/Checkpoint">000B77</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Checkpoint">000B77</idno><idno type="wicri:source">PubMed</idno><idno type="wicri:Area/PubMed/Corpus">000F48</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000F48</idno><idno type="wicri:Area/PubMed/Curation">000F48</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">000F48</idno><idno type="wicri:Area/PubMed/Checkpoint">000F48</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">000F48</idno><idno type="wicri:Area/Ncbi/Merge">000960</idno><idno type="wicri:Area/Ncbi/Curation">000960</idno><idno type="wicri:Area/Ncbi/Checkpoint">000960</idno><idno type="wicri:Area/Main/Merge">002397</idno><idno type="wicri:Area/Main/Curation">002206</idno><idno type="wicri:Area/Main/Exploration">002206</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Differential regulation of wild-type and mutant alpha-synuclein binding to synaptic membranes by cytosolic factors</title><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="4"><nlm:aff id="I1">Centre for Research in Neurodegenerative Diseases, University of Toronto, Toronto, Ontario, M5S 3H2 Canada</nlm:aff><orgName type="university">Université de Toronto</orgName><country>Canada</country><placeName><settlement type="city">Toronto</settlement><region type="state">Ontario</region></placeName></affiliation><affiliation wicri:level="4"><nlm:aff id="I2">Centre for Cellular and Molecular Neurobiology, University of Liege, 4000 Liege, Belgium</nlm:aff><country xml:lang="fr">Belgique</country><wicri:regionArea>Centre for Cellular and Molecular Neurobiology, University of Liege, 4000 Liege</wicri:regionArea><placeName><region type="province" nuts="2">Province de Liège</region><settlement type="city">Liège</settlement><settlement type="city">Liège</settlement></placeName><orgName type="university">Université de Liège</orgName></affiliation></author><author><name sortKey="Visanji, Naomi P" sort="Visanji, Naomi P" uniqKey="Visanji N" first="Naomi P" last="Visanji">Naomi P. Visanji</name><affiliation wicri:level="4"><nlm:aff id="I1">Centre for Research in Neurodegenerative Diseases, University of Toronto, Toronto, Ontario, M5S 3H2 Canada</nlm:aff><orgName type="university">Université de Toronto</orgName><country>Canada</country><placeName><settlement type="city">Toronto</settlement><region type="state">Ontario</region></placeName></affiliation></author><author><name sortKey="Whitehead, Shawn N" sort="Whitehead, Shawn N" uniqKey="Whitehead S" first="Shawn N" last="Whitehead">Shawn N. Whitehead</name><affiliation wicri:level="1"><nlm:aff id="I3">Neural Regeneration Laboratory, Ottawa Institute of Systems Biology, Department of Biochemistry, Microbiology, and Immunology, University of Ottawa, Ottawa, K1H 8M5, Canada</nlm:aff><country xml:lang="fr">Canada</country><wicri:regionArea>Neural Regeneration Laboratory, Ottawa Institute of Systems Biology, Department of Biochemistry, Microbiology, and Immunology, University of Ottawa, Ottawa, K1H 8M5</wicri:regionArea><wicri:noRegion>K1H 8M5</wicri:noRegion></affiliation><affiliation wicri:level="1"><nlm:aff id="I4">Institute for Biological Sciences, National Research Council of Canada, Ottawa, K1A 0R6, Canada</nlm:aff><country xml:lang="fr">Canada</country><wicri:regionArea>Institute for Biological Sciences, National Research Council of Canada, Ottawa, K1A 0R6</wicri:regionArea><wicri:noRegion>K1A 0R6</wicri:noRegion></affiliation></author><author><name sortKey="Marsilio, Diana" sort="Marsilio, Diana" uniqKey="Marsilio D" first="Diana" last="Marsilio">Diana Marsilio</name><affiliation wicri:level="4"><nlm:aff id="I1">Centre for Research in Neurodegenerative Diseases, University of Toronto, Toronto, Ontario, M5S 3H2 Canada</nlm:aff><orgName type="university">Université de Toronto</orgName><country>Canada</country><placeName><settlement type="city">Toronto</settlement><region type="state">Ontario</region></placeName></affiliation></author><author><name sortKey="Hou, Weimin" sort="Hou, Weimin" uniqKey="Hou W" first="Weimin" last="Hou">Weimin Hou</name><affiliation wicri:level="1"><nlm:aff id="I3">Neural Regeneration Laboratory, Ottawa Institute of Systems Biology, Department of Biochemistry, Microbiology, and Immunology, University of Ottawa, Ottawa, K1H 8M5, Canada</nlm:aff><country xml:lang="fr">Canada</country><wicri:regionArea>Neural Regeneration Laboratory, Ottawa Institute of Systems Biology, Department of Biochemistry, Microbiology, and Immunology, University of Ottawa, Ottawa, K1H 8M5</wicri:regionArea><wicri:noRegion>K1H 8M5</wicri:noRegion></affiliation></author><author><name sortKey="Figeys, Daniel" sort="Figeys, Daniel" uniqKey="Figeys D" first="Daniel" last="Figeys">Daniel Figeys</name><affiliation wicri:level="1"><nlm:aff id="I3">Neural Regeneration Laboratory, Ottawa Institute of Systems Biology, Department of Biochemistry, Microbiology, and Immunology, University of Ottawa, Ottawa, K1H 8M5, Canada</nlm:aff><country xml:lang="fr">Canada</country><wicri:regionArea>Neural Regeneration Laboratory, Ottawa Institute of Systems Biology, Department of Biochemistry, Microbiology, and Immunology, University of Ottawa, Ottawa, K1H 8M5</wicri:regionArea><wicri:noRegion>K1H 8M5</wicri:noRegion></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 wicri:level="4"><nlm:aff id="I1">Centre for Research in Neurodegenerative Diseases, University of Toronto, Toronto, Ontario, M5S 3H2 Canada</nlm:aff><orgName type="university">Université de Toronto</orgName><country>Canada</country><placeName><settlement type="city">Toronto</settlement><region type="state">Ontario</region></placeName></affiliation></author><author><name sortKey="Bennett, Steffany Al" sort="Bennett, Steffany Al" uniqKey="Bennett S" first="Steffany Al" last="Bennett">Steffany Al Bennett</name><affiliation wicri:level="1"><nlm:aff id="I3">Neural Regeneration Laboratory, Ottawa Institute of Systems Biology, Department of Biochemistry, Microbiology, and Immunology, University of Ottawa, Ottawa, K1H 8M5, Canada</nlm:aff><country xml:lang="fr">Canada</country><wicri:regionArea>Neural Regeneration Laboratory, Ottawa Institute of Systems Biology, Department of Biochemistry, Microbiology, and Immunology, University of Ottawa, Ottawa, K1H 8M5</wicri:regionArea><wicri:noRegion>K1H 8M5</wicri:noRegion></affiliation></author><author><name sortKey="Tandon, Anurag" sort="Tandon, Anurag" uniqKey="Tandon A" first="Anurag" last="Tandon">Anurag Tandon</name><affiliation wicri:level="4"><nlm:aff id="I1">Centre for Research in Neurodegenerative Diseases, University of Toronto, Toronto, Ontario, M5S 3H2 Canada</nlm:aff><orgName type="university">Université de Toronto</orgName><country>Canada</country><placeName><settlement type="city">Toronto</settlement><region type="state">Ontario</region></placeName></affiliation></author></analytic><series><title level="j">BMC Neuroscience</title><idno type="eISSN">1471-2202</idno><imprint><date when="2008">2008</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Adenosine Triphosphate (analysis)</term><term>Adenosine Triphosphate (metabolism)</term><term>Animals</term><term>Blotting, Western</term><term>Brain Chemistry</term><term>Calcium (analysis)</term><term>Calcium (metabolism)</term><term>Cytosol (chemistry)</term><term>Cytosol (metabolism)</term><term>Genotype</term><term>Humans</term><term>Lipids (analysis)</term><term>Membrane Proteins (chemistry)</term><term>Membrane Proteins (genetics)</term><term>Membrane Proteins (metabolism)</term><term>Mice</term><term>Mice, Knockout</term><term>Mutation</term><term>Mutation, Missense</term><term>Parkinson Disease (genetics)</term><term>Parkinson Disease (metabolism)</term><term>Platelet Activating Factor (analogs & derivatives)</term><term>Platelet Activating Factor (analysis)</term><term>Platelet Activating Factor (metabolism)</term><term>Protein Binding</term><term>Synaptic Membranes (metabolism)</term><term>Synaptosomes (metabolism)</term><term>alpha-Synuclein (analysis)</term><term>alpha-Synuclein (genetics)</term><term>alpha-Synuclein (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analogs & derivatives" xml:lang="en"><term>Platelet Activating Factor</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Adenosine Triphosphate</term><term>Calcium</term><term>Lipids</term><term>Platelet Activating Factor</term><term>alpha-Synuclein</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Membrane Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Membrane Proteins</term><term>alpha-Synuclein</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Adenosine Triphosphate</term><term>Calcium</term><term>Membrane Proteins</term><term>Platelet Activating Factor</term><term>alpha-Synuclein</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Cytosol</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Parkinson Disease</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Cytosol</term><term>Parkinson Disease</term><term>Synaptic Membranes</term><term>Synaptosomes</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Blotting, Western</term><term>Brain Chemistry</term><term>Genotype</term><term>Humans</term><term>Mice</term><term>Mice, Knockout</term><term>Mutation</term><term>Mutation, Missense</term><term>Protein Binding</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><sec><title>Background</title><p>Alpha-Synuclein (α-syn), a 140 amino acid protein associated with presynaptic membranes in brain, is a major constituent of Lewy bodies in Parkinson's disease (PD). Three missense mutations (A30P, A53T and E46K) in the α-syn gene are associated with rare autosomal dominant forms of familial PD. However, the regulation of α-syn's cellular localization in neurons and the effects of the PD-linked mutations are poorly understood.</p></sec><sec><title>Results</title><p>In the present study, we analysed the ability of cytosolic factors to regulate α-syn binding to synaptic membranes. We show that co-incubation with brain cytosol significantly increases the membrane binding of normal and PD-linked mutant α-syn. To characterize cytosolic factor(s) that modulate α-syn binding properties, we investigated the ability of proteins, lipids, ATP and calcium to modulate α-syn membrane interactions. We report that lipids and ATP are two of the principal cytosolic components that modulate Wt and A53T α-syn binding to the synaptic membrane. We further show that 1-O-hexadecyl-2-acetyl-<italic>sn</italic>-glycero-3-phosphocholine (C16:0 PAF) is one of the principal lipids found in complex with cytosolic proteins and is required to enhance α-syn interaction with synaptic membrane. In addition, the impaired membrane binding observed for A30P α-syn was significantly mitigated by the presence of protease-sensitive factors in brain cytosol.</p></sec><sec><title>Conclusion</title><p>These findings suggest that endogenous brain cytosolic factors regulate Wt and mutant α-syn membrane binding, and could represent potential targets to influence α-syn solubility in brain.</p></sec></div></front><back><div1 type="bibliography"><listBibl><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct></listBibl></div1></back></TEI><affiliations><list><country><li>Belgique</li><li>Canada</li></country><region><li>Ontario</li><li>Province de Liège</li></region><settlement><li>Liège</li><li>Toronto</li></settlement><orgName><li>Université de Liège</li><li>Université de Toronto</li></orgName></list><tree><country name="Canada"><region name="Ontario"><name sortKey="Wislet Gendebien, Sabine" sort="Wislet Gendebien, Sabine" uniqKey="Wislet Gendebien S" first="Sabine" last="Wislet-Gendebien">Sabine Wislet-Gendebien</name></region><name sortKey="Bennett, Steffany Al" sort="Bennett, Steffany Al" uniqKey="Bennett S" first="Steffany Al" last="Bennett">Steffany Al Bennett</name><name sortKey="Figeys, Daniel" sort="Figeys, Daniel" uniqKey="Figeys D" first="Daniel" last="Figeys">Daniel Figeys</name><name sortKey="Fraser, Paul E" sort="Fraser, Paul E" uniqKey="Fraser P" first="Paul E" last="Fraser">Paul E. Fraser</name><name sortKey="Hou, Weimin" sort="Hou, Weimin" uniqKey="Hou W" first="Weimin" last="Hou">Weimin Hou</name><name sortKey="Marsilio, Diana" sort="Marsilio, Diana" uniqKey="Marsilio D" first="Diana" last="Marsilio">Diana Marsilio</name><name sortKey="Tandon, Anurag" sort="Tandon, Anurag" uniqKey="Tandon A" first="Anurag" last="Tandon">Anurag Tandon</name><name sortKey="Visanji, Naomi P" sort="Visanji, Naomi P" uniqKey="Visanji N" first="Naomi P" last="Visanji">Naomi P. Visanji</name><name sortKey="Whitehead, Shawn N" sort="Whitehead, Shawn N" uniqKey="Whitehead S" first="Shawn N" last="Whitehead">Shawn N. Whitehead</name><name sortKey="Whitehead, Shawn N" sort="Whitehead, Shawn N" uniqKey="Whitehead S" first="Shawn N" last="Whitehead">Shawn N. Whitehead</name></country><country name="Belgique"><region name="Province de Liège"><name sortKey="Wislet Gendebien, Sabine" sort="Wislet Gendebien, Sabine" uniqKey="Wislet Gendebien S" first="Sabine" last="Wislet-Gendebien">Sabine Wislet-Gendebien</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:18808659" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a ParkinsonCanadaV1
| This area was generated with Dilib version V0.6.29. |  |