Effect of Ser-129 phosphorylation on interaction of α-synuclein with synaptic and cellular membranes.
Identifieur interne : 000B63 ( PubMed/Curation ); précédent : 000B62; suivant : 000B64Effect of Ser-129 phosphorylation on interaction of α-synuclein with synaptic and cellular membranes.
Auteurs : Naomi P. Visanji [Canada] ; Sabine Wislet-Gendebien ; Loren W. Oschipok ; Gang Zhang ; Isabelle Aubert ; Paul E. Fraser ; Anurag TandonSource :
- The Journal of biological chemistry [ 1083-351X ] ; 2011.
English descriptors
- KwdEn :
- Amino Acid Substitution, Animals, Cell Line, Epitopes (genetics), Epitopes (metabolism), Humans, Lewy Bodies (genetics), Lewy Bodies (metabolism), Mice, Mice, Knockout, Mutation, Missense, Parkinsonian Disorders (genetics), Parkinsonian Disorders (metabolism), Protein Binding (genetics), Protein Kinases (biosynthesis), Protein Kinases (genetics), Protein Transport (genetics), Protein-Serine-Threonine Kinases (biosynthesis), Protein-Serine-Threonine Kinases (genetics), Synaptic Membranes (genetics), Synaptic Membranes (metabolism), alpha-Synuclein (genetics), alpha-Synuclein (metabolism).
- MESH :
- chemical , biosynthesis : Protein Kinases, Protein-Serine-Threonine Kinases.
- chemical , genetics : Epitopes, Protein Kinases, Protein-Serine-Threonine Kinases, alpha-Synuclein.
- chemical , metabolism : Epitopes, alpha-Synuclein.
- genetics : Lewy Bodies, Parkinsonian Disorders, Protein Binding, Protein Transport, Synaptic Membranes.
- metabolism : Lewy Bodies, Parkinsonian Disorders, Synaptic Membranes.
- Amino Acid Substitution, Animals, Cell Line, Humans, Mice, Mice, Knockout, Mutation, Missense.
Abstract
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.
DOI: 10.1074/jbc.M111.253450
PubMed: 21849493
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<term>Epitopes (metabolism)</term>
<term>Humans</term>
<term>Lewy Bodies (genetics)</term>
<term>Lewy Bodies (metabolism)</term>
<term>Mice</term>
<term>Mice, Knockout</term>
<term>Mutation, Missense</term>
<term>Parkinsonian Disorders (genetics)</term>
<term>Parkinsonian Disorders (metabolism)</term>
<term>Protein Binding (genetics)</term>
<term>Protein Kinases (biosynthesis)</term>
<term>Protein Kinases (genetics)</term>
<term>Protein Transport (genetics)</term>
<term>Protein-Serine-Threonine Kinases (biosynthesis)</term>
<term>Protein-Serine-Threonine Kinases (genetics)</term>
<term>Synaptic Membranes (genetics)</term>
<term>Synaptic Membranes (metabolism)</term>
<term>alpha-Synuclein (genetics)</term>
<term>alpha-Synuclein (metabolism)</term>
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<keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Protein Kinases</term>
<term>Protein-Serine-Threonine Kinases</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Epitopes</term>
<term>Protein Kinases</term>
<term>Protein-Serine-Threonine Kinases</term>
<term>alpha-Synuclein</term>
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<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Epitopes</term>
<term>alpha-Synuclein</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Lewy Bodies</term>
<term>Parkinsonian Disorders</term>
<term>Protein Binding</term>
<term>Protein Transport</term>
<term>Synaptic Membranes</term>
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<term>Parkinsonian Disorders</term>
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<term>Animals</term>
<term>Cell Line</term>
<term>Humans</term>
<term>Mice</term>
<term>Mice, Knockout</term>
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<front><div type="abstract" xml:lang="en">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.</div>
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<Abstract><AbstractText>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.</AbstractText>
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<PMID Version="1">12377775</PMID>
</CommentsCorrections>
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