La maladie de Parkinson en France (serveur d'exploration)

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Rat α-synuclein interacts with Tat binding protein 1, a component of the 26S proteasomal complex

Identifieur interne : 004219 ( Main/Merge ); précédent : 004218; suivant : 004220

Rat α-synuclein interacts with Tat binding protein 1, a component of the 26S proteasomal complex

Auteurs : Medeva Ghee [France] ; Alain Fournier [France] ; Jacques Mallet [France]

Source :

RBID : Pascal:01-0080368

Descripteurs français

English descriptors

Abstract

The α-synuclein gene, which encodes a brain presynaptic nerve terminal protein of unknown function, is linked to familial early-onset Parkinson's disease (PD). The finding that α-synuclein forms the major fibrillary component of Lewy bodies in brains of PD patients suggests that the two point mutations in α-synuclein (Ala53Thr, Ala30Pro) may promote the aggregation of α-synuclein into filaments. To address the role of α-synuclein in neurodegenerative diseases, we performed a yeast two-hybrid screen of a rat adult brain cDNA library using rat α-synuclein 2 (aSYN2). Here we report that aSYN2 interacts specifically with Tat binding protein 1, a subunit of the 700-kDa proteasome activator (PA700), the regulatory complex of the 26S proteasome and of the modulator complex, which enhances PA700 activation of the proteasome.

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Pascal:01-0080368

Le document en format XML

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<div type="abstract" xml:lang="en">The α-synuclein gene, which encodes a brain presynaptic nerve terminal protein of unknown function, is linked to familial early-onset Parkinson's disease (PD). The finding that α-synuclein forms the major fibrillary component of Lewy bodies in brains of PD patients suggests that the two point mutations in α-synuclein (Ala
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