Rat α‐Synuclein Interacts with Tat Binding Protein 1, a Component of the 26S Proteasomal Complex

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 (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.