| Literature DB >> 21798244 |
Hak Joo Lee1, Shin Jung Kang, Kyunghee Lee, Hana Im.
Abstract
α-Synuclein has been implicated in the pathogenesis of Parkinson's disease. Although it is highly conserved, its physiological function has not yet been elucidated in detail. In an effort to define the function of α-synuclein, interacting proteins were screened in phage display assays. Prenylated Rab acceptor protein 1 (PRA1) was identified as an interacting partner. A selective interaction between α-synuclein and PRA1 was confirmed by coimmunoprecipitation and GST pull-down assays. PRA1 and α-synuclein were colocalized in N2a neuronal cells. Cotransfection of α-synuclein and PRA1 caused vesicles to accumulate in the periphery of the cytosol in neuronal cells, suggesting that overexpression of α-synuclein hinders proper vesicle trafficking and recycling as a result of the interaction between α-synuclein and PRA1.Entities:
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Year: 2011 PMID： 21798244 DOI： 10.1016/j.bbrc.2011.07.028
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN： 0006-291X Impact factor: 3.575