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α-Synuclein modifies huntingtin aggregation in living cells

Lookup NU author(s): Professor Tiago OuteiroORCiD

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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. Structured summary of protein interactions: Htt and Htt physically interact by bimolecular fluorescence complementation (View interaction) alpha-syn and Htt physically interact by bimolecular fluorescence complementation (View interaction) alpha-syn and alpha-syn physically interact by comigration in non-denaturing gel electrophoresis (View interaction) Htt and Htt physically interact by comigration in non-denaturing gel electrophoresis (View interaction) alpha-syn and Htt colocalize by fluorescence microscopy (View Interaction: 1, 2) alpha-syn and alpha-syn physically interact by bimolecular fluorescence complementation (View interaction) Htt and alpha-syn physically interact by comigration in non-denaturing gel electrophoresis (View interaction) © 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.


Publication metadata

Author(s): Herrera F, Outeiro TF

Publication type: Article

Publication status: Published

Journal: FEBS Letters

Year: 2012

Volume: 586

Issue: 1

Pages: 7-12

Print publication date: 02/01/2012

Online publication date: 24/11/2011

ISSN (print): 0014-5793

ISSN (electronic): 1873-3468

Publisher: John Wiley & Sons Ltd

URL: https://doi.org/10.1016/j.febslet.2011.11.019

DOI: 10.1016/j.febslet.2011.11.019

PubMed id: 22119730


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