α-Synuclein phosphorylation as a therapeutic target in Parkinson’s disease
Identifieur interne : 000049 ( Main/Exploration ); précédent : 000048; suivant : 000050α-Synuclein phosphorylation as a therapeutic target in Parkinson’s disease
Auteurs : Steven P. Braithwaite [États-Unis] ; Jeffry B. Stock ; M. Maral Mouradian [États-Unis]Source :
- Reviews in the Neurosciences [ 0334-1763 ] ; 2012-04-01.
Abstract
Phosphorylation is a key post-translational modification necessary for normal cellular signaling and, therefore, lies at the heart of cellular function. In neurodegenerative disorders, abnormal hyperphosphorylation of pathogenic proteins is a common phenomenon that contributes in important ways to the disease process. A prototypical protein that is hyperphosphorylated in the brain is α-synuclein (α-syn) – found in Lewy bodies and Lewy neurites – the pathological hallmarks of Parkinson’s disease (PD) and other α-synucleinopathies. The genetic linkage of α-syn to PD as well as its pathological association in both genetic and sporadic cases have made it the primary protein of interest. In understanding how α-syn dysfunction occurs, increasing focus is being placed on its abnormal aggregation and the contribution of phosphorylation to this process. Studies of both the kinases and phosphatases that regulate α-syn phosphorylation are beginning to reveal the roles of this post-translational modification in disease pathogenesis. Modulation of α-syn phosphorylation may ultimately prove to be a viable strategy for disease-modifying therapeutic interventions. In this review, we explore mechanisms related to α-syn phosphorylation, its biophysical and functional consequences, and its role in neurodegeneration.
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DOI: 10.1515/revneuro-2011-0067
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In neurodegenerative disorders, abnormal hyperphosphorylation of pathogenic proteins is a common phenomenon that contributes in important ways to the disease process. A prototypical protein that is hyperphosphorylated in the brain is α-synuclein (α-syn) – found in Lewy bodies and Lewy neurites – the pathological hallmarks of Parkinson’s disease (PD) and other α-synucleinopathies. The genetic linkage of α-syn to PD as well as its pathological association in both genetic and sporadic cases have made it the primary protein of interest. In understanding how α-syn dysfunction occurs, increasing focus is being placed on its abnormal aggregation and the contribution of phosphorylation to this process. Studies of both the kinases and phosphatases that regulate α-syn phosphorylation are beginning to reveal the roles of this post-translational modification in disease pathogenesis. Modulation of α-syn phosphorylation may ultimately prove to be a viable strategy for disease-modifying therapeutic interventions. In this review, we explore mechanisms related to α-syn phosphorylation, its biophysical and functional consequences, and its role in neurodegeneration.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>New Jersey</li></region></list><tree><noCountry><name sortKey="Stock, Jeffry B" sort="Stock, Jeffry B" uniqKey="Stock J" first="Jeffry B." last="Stock">Jeffry B. Stock</name></noCountry><country name="États-Unis"><region name="New Jersey"><name sortKey="Braithwaite, Steven P" sort="Braithwaite, Steven P" uniqKey="Braithwaite S" first="Steven P." last="Braithwaite">Steven P. Braithwaite</name></region><name sortKey="Mouradian, M Maral" sort="Mouradian, M Maral" uniqKey="Mouradian M" first="M. Maral" last="Mouradian">M. Maral Mouradian</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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