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Rat α‐Synuclein Interacts with Tat Binding Protein 1, a Component of the 26S Proteasomal Complex
Author(s) -
Ghee Medeva,
Fournier Alain,
Mallet Jacques
Publication year - 2000
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1046/j.1471-4159.2000.0752221.x
Subject(s) - alpha synuclein , proteasome , microbiology and biotechnology , protein subunit , biology , synuclein , activator (genetics) , lewy body , parkinson's disease , gene , biochemistry , medicine , disease
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 53 Thr, Ala 30 Pro) 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 (αSYN2). Here we report that αSYN2 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.