Ataxin-2 Interacts with the Dead/H-box Rna Helicase Ddx6 and Interferes with P-bodies and Stress Granules.
From: Max Planck Institute for Molecular Genetics, 14195 Berlin, Germany.
Molecular biology of the cell
- Publish Date: Apr 2007
- ISSN: 1059-1524
- Volume: 18
- Issue: 4
- Pages: 1385-96
- Medium: Print
- Language: English
- Citation (JAMA): Nonhoff Ute, Ralser Markus, Welzel Franziska, et al. Ataxin-2 Interacts with the Dead/H-box Rna Helicase Ddx6 and Interferes with P-bodies and Stress Granules.. Mol. Biol. Cell Apr 2007;18:1385-96
Abstract
Tight control of translation is fundamental for eukaryotic cells, and deregulation of proteins implicated contributes to numerous human diseases. The neurodegenerative disorder spinocerebellar ataxia type 2 is caused by a trinucleotide expansion in the SCA2 gene encoding a lengthened polyglutamine stretch in the gene product ataxin-2, which seems to be implicated in cellular RNA-processing pathways and translational regulation. Here, we substantiate a function of ataxin-2 in such pathways by demonstrating that ataxin-2 interacts with the DEAD/H-box RNA helicase DDX6, a component of P-bodies and stress granules, representing cellular structures of mRNA triage. We discovered that altered ataxin-2 levels interfere with the assembly of stress granules and cellular P-body structures. Moreover, ataxin-2 regulates the intracellular concentration of its interaction partner, the poly(A)-binding protein, another stress granule component and a key factor for translational control. Thus, our data imply that the cellular ataxin-2 concentration is important for the assembly of stress granules and P-bodies, which are main compartments for regulating and controlling mRNA degradation, stability, and translation.
Mesh Headings (Keywords): Cells, Cultured, Cytoplasmic Granules, DEAD-box RNA Helicases, Humans, Microbodies, Nerve Tissue Proteins, Poly(A)-Binding Proteins, Protein Structure, Tertiary, Proto-Oncogene Proteins
Check for Full Text / PubMed Unique Identifier (PMID): 17392519
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