La maladie de Parkinson au Canada (serveur d'exploration)

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Effect of Ser-129 Phosphorylation on Interaction of α-Synuclein with Synaptic and Cellular Membranes*

Identifieur interne : 001678 ( Main/Exploration ); précédent : 001677; suivant : 001679

Effect 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 :

RBID : PMC:3195582

English descriptors

Abstract

Background: The majority of α-synuclein is phosphorylated at serine 129 in Lewy bodies.

Results: The membrane association of PD-linked mutant α-synuclein, but not wild-type α-synuclein, was increased by serine 129 phosphorylation.

Conclusion: Pathological serine 129 phosphorylation regulates membrane accumulation of mutant α-synuclein.

Significance: 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.


Url:
DOI: 10.1074/jbc.M111.253450
PubMed: 21849493
PubMed Central: 3195582


Affiliations:


Links toward previous steps (curation, corpus...)


Le document en format XML

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<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>
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