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  An integrative approach to gain insights into the cellular function of human ataxin-2

Ralser, M., Albrecht, M., Nonhoff, U., Lengauer, T., Lehrach, H., & Krobitsch, S. (2005). An integrative approach to gain insights into the cellular function of human ataxin-2. Journal of Molecular Biology (London), 346(1), 203-214. doi:10.1016/j.jmb.2004.11.024.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-86DE-D Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-86DF-B
Genre: Journal Article
Alternative Title : J Mol Biol

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 Creators:
Ralser, Markus1, Author              
Albrecht, Mario, Author
Nonhoff, Ute1, Author              
Lengauer, Thomas, 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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Free keywords: polyglutamine disorder; spinocerebellar ataxia type 2; ataxin-2; Pbp1; poly(A)-binding protein
 Abstract: Spinocerebellar ataxia type 2 (SCA2) is a hereditary neurodegenerative disorder caused by a trinucleotide expansion in the SCA2 gene, encoding a polyglutamine stretch in the gene product ataxin-2 (ATX2), whose cellular function is unknown. However, ATX2 interacts with A2BP1, a protein containing an RNA-recognition motif, and the existence of an interaction motif for the C-terminal domain of the poly(A)-binding protein (PABC) as well as an Lsm (Like Sm) domain in ATX2 suggest that ATX2 like its yeast homolog Pbp1 might be involved in RNA metabolism. Here, we show that, similar to Pbp1, ATX2 suppresses the petite (pet−) phenotype of Δmrs2 yeast strains lacking mitochondrial group II introns. This finding points to a close functional relationship between the two homologs. To gain insight into potential functions of ATX2, we also generated a comprehensive protein interaction network for Pbp1 from publicly available databases, which implicates Pbp1 in diverse RNA-processing pathways. The functional relationship of ATX2 and Pbp1 is further corroborated by the experimental confirmation of the predicted interaction of ATX2 with the cytoplasmic poly(A)-binding protein 1 (PABP) using yeast-2-hybrid analysis as well as co-immunoprecipitation experiments. Immunofluorescence studies revealed that ATX2 and PABP co-localize in mammalian cells, remarkably, even under conditions in which PABP accumulates in distinct cytoplasmic foci representing sites of mRNA triage.

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Language(s): eng - English
 Dates: 2005-02-11
 Publication Status: Published in print
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 Rev. Type: -
 Identifiers: eDoc: 273070
DOI: 10.1016/j.jmb.2004.11.024
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Title: Journal of Molecular Biology (London)
  Alternative Title : J Mol Biol
Source Genre: Journal
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Pages: - Volume / Issue: 346 (1) Sequence Number: - Start / End Page: 203 - 214 Identifier: ISSN: 0022-2836