Abstract:
:Several neurodegenerative disorders are characterized by the accumulation of proteinaceous inclusions in the central nervous system. These inclusions are frequently composed of a mixture of aggregation-prone proteins. Here, we used a bimolecular fluorescence complementation assay to study the initial steps of the co-aggregation of huntingtin (Htt) and α-synuclein (α-syn), two aggregation-prone proteins involved in Huntington's disease (HD) and Parkinson's disease (PD), respectively. We found that Htt (exon 1) oligomerized with α-syn and sequestered it in the cytosol. In turn, α-syn increased the number of cells displaying aggregates, decreased the number of aggregates per cell and increased the average size of the aggregates. Our results support the idea that co-aggregation of aggregation-prone proteins can contribute to the histopathology of neurodegenerative disorders.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Herrera F,Outeiro TFdoi
10.1016/j.febslet.2011.11.019subject
Has Abstractpub_date
2012-01-02 00:00:00pages
7-12issue
1eissn
0014-5793issn
1873-3468pii
S0014-5793(11)00844-1journal_volume
586pub_type
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