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  Ataxin-2 and huntingtin interact with endophilin-A complexes to function in plastin-associated pathways

Ralser, M., Nonhoff, U., Albrecht, M., Lengauer, T., Wanker, E. E., Lehrach, H., et al. (2005). Ataxin-2 and huntingtin interact with endophilin-A complexes to function in plastin-associated pathways. Human Molecular Genetics, 14(19), 2893-2909. doi:10.1093/hmg/ddi321.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-85BB-5 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-85BC-3
Genre: Journal Article
Alternative Title : Hum Mol Genet

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 Creators:
Ralser, Markus1, Author              
Nonhoff, Ute1, Author              
Albrecht, Mario, Author
Lengauer, Thomas, Author
Wanker, Erich E., Author
Lehrach, Hans1, Author              
Krobitsch, Sylvia2, Author              
Affiliations:
1Dept. of Vertebrate Genomics (Head: Hans Lehrach), Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1433550              
2Neurodegenerative Disorders (Sylvia Krobitsch), Independent Junior Research Groups (OWL), Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1479661              

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 Abstract: Spinocerebellar ataxia type 2 is an inherited neurodegenerative disorder that is caused by an expanded trinucleotide repeat in the SCA2 gene, encoding a polyglutamine stretch in the gene product ataxin-2. Although evidence has been provided that ataxin-2 is involved in RNA metabolism, the physiological function of ataxin-2 remains unclear. Here, we demonstrate that ataxin-2 interacts with two members of the endophilin family, endophilin-A1 and endophilin-A3. To elucidate the physiological implications of these interactions, we exploited yeast as a model system and discovered that expression of ataxin-2 as well as both endophilin proteins is toxic for yeast lacking the SAC6 gene product fimbrin, a protein involved in actin filament organization and endocytotic processes. Intriguingly, expression of huntingtin, another polyglutamine protein interacting with endophilin-A3, was also toxic in {Delta}sac6 yeast. These effects can be suppressed by simultaneous expression of one of the two human fimbrin orthologs, L- or T-plastin. Moreover, we have discovered that ataxin-2 associates with L- and T-plastin and that overexpression of ataxin-2 leads to accumulation of T-plastin in mammalian cells. Thus, our findings suggest an interplay between ataxin-2, endophilin proteins and huntingtin in plastin-associated cellular pathways.

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Language(s): eng - English
 Dates: 2005-08-22
 Publication Status: Published in print
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 Identifiers: eDoc: 273081
DOI: 10.1093/hmg/ddi321
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Title: Human Molecular Genetics
  Alternative Title : Hum Mol Genet
Source Genre: Journal
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Pages: - Volume / Issue: 14 (19) Sequence Number: - Start / End Page: 2893 - 2909 Identifier: ISSN: 0964-6906