| pubmed-article:16835262 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16835262 | lifeskim:mentions | umls-concept:C0032592 | lld:lifeskim |
| pubmed-article:16835262 | lifeskim:mentions | umls-concept:C0013138 | lld:lifeskim |
| pubmed-article:16835262 | lifeskim:mentions | umls-concept:C0531288 | lld:lifeskim |
| pubmed-article:16835262 | lifeskim:mentions | umls-concept:C1538299 | lld:lifeskim |
| pubmed-article:16835262 | lifeskim:mentions | umls-concept:C1706853 | lld:lifeskim |
| pubmed-article:16835262 | lifeskim:mentions | umls-concept:C1334043 | lld:lifeskim |
| pubmed-article:16835262 | pubmed:issue | 16 | lld:pubmed |
| pubmed-article:16835262 | pubmed:dateCreated | 2006-7-31 | lld:pubmed |
| pubmed-article:16835262 | pubmed:abstractText | Mutations resulting in the expansion of a polyglutamine tract in the protein ataxin-2 give rise to the neurodegenerative disorders spinocerebellar ataxia type 2 and Parkinson's disease. The normal cellular function of ataxin-2 and the mechanism by which polyglutamine expansion of ataxin-2 causes neurodegeneration are unknown. Here, we demonstrate that ataxin-2 and its Drosophila homolog, ATX2, assemble with polyribosomes and poly(A)-binding protein (PABP), a key regulator of mRNA translation. The assembly of ATX2 with polyribosomes is mediated independently by two distinct evolutionarily conserved regions of ATX2: an N-terminal Lsm/Lsm-associated domain (LsmAD), found in proteins that function in nuclear RNA processing and mRNA decay, and a PAM2 motif, found in proteins that interact physically with PABP. We further show that the PAM2 motif mediates a physical interaction of ATX2 with PABP in addition to promoting ATX2 assembly with polyribosomes. Our results suggest a model in which ATX2 binds mRNA directly through its Lsm/LsmAD domain and indirectly via binding PABP that is itself directly bound to mRNA. These findings, coupled with work on other ataxin-2 family members, suggest that ATX2 plays a direct role in translational regulation. Our results raise the possibility that polyglutamine expansions within ataxin-2 cause neurodegeneration by interfering with the translational regulation of particular mRNAs. | lld:pubmed |
| pubmed-article:16835262 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16835262 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16835262 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16835262 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16835262 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16835262 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16835262 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16835262 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16835262 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16835262 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16835262 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16835262 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16835262 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:16835262 | pubmed:issn | 0964-6906 | lld:pubmed |
| pubmed-article:16835262 | pubmed:author | pubmed-author:SatterfieldTe... | lld:pubmed |
| pubmed-article:16835262 | pubmed:author | pubmed-author:PallanckLeo... | lld:pubmed |
| pubmed-article:16835262 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16835262 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:16835262 | pubmed:volume | 15 | lld:pubmed |
| pubmed-article:16835262 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16835262 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16835262 | pubmed:pagination | 2523-32 | lld:pubmed |
| pubmed-article:16835262 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:16835262 | pubmed:meshHeading | pubmed-meshheading:16835262... | lld:pubmed |
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| pubmed-article:16835262 | pubmed:meshHeading | pubmed-meshheading:16835262... | lld:pubmed |
| pubmed-article:16835262 | pubmed:meshHeading | pubmed-meshheading:16835262... | lld:pubmed |
| pubmed-article:16835262 | pubmed:meshHeading | pubmed-meshheading:16835262... | lld:pubmed |
| pubmed-article:16835262 | pubmed:meshHeading | pubmed-meshheading:16835262... | lld:pubmed |
| pubmed-article:16835262 | pubmed:meshHeading | pubmed-meshheading:16835262... | lld:pubmed |
| pubmed-article:16835262 | pubmed:meshHeading | pubmed-meshheading:16835262... | lld:pubmed |
| pubmed-article:16835262 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16835262 | pubmed:articleTitle | Ataxin-2 and its Drosophila homolog, ATX2, physically assemble with polyribosomes. | lld:pubmed |
| pubmed-article:16835262 | pubmed:affiliation | Department of Genome Sciences, University of Washington School of Medicine, Seattle, WA 98195-7730, USA. | lld:pubmed |
| pubmed-article:16835262 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16835262 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:16835262 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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