| http://purl.uniprot.org/citations/20637808 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/20637808 | http://www.w3.org/2000/01/rdf-schema#comment | "Ataxin-3 (ATXN3) is a widely expressed protein that binds to ubiquitylated proteins, has deubiquitylating activity in vitro and is thought to modulate substrate degradation through the ubiquitin-proteasome pathway. Expansion of a polyglutamine tract in ATXN3 causes Machado-Joseph disease, a late-onset neurodegenerative disorder characterized by ubiquitin-positive aggregate formation and specific neuronal death. Although ATXN3 has been involved in transcriptional repression and in the ubiquitin-proteasome pathway, its biological function is still unknown. In this work, we show that depletion of ATXN3 using small-interference RNA (siRNA) causes a prominent phenotype in both human and mouse cell lines. A mild increase in ubiquitylation occurs and cells exhibit ubiquitin-positive foci, which is consistent with ATXN3 putative function as a deubiquitylating enzyme. In addition, siATXN3-silenced cells exhibit marked morphological changes such as rounder shape and loss of adhesion protrusions. At a structural level, the microtubule, microfilament and intermediate filament networks are severely compromised and disorganized. This cytoskeletal phenotype is reversible and dependent on ATXN3 levels. Cell-extracellular matrix connection is also affected in ATXN3-depleted cells as talin expression is reduced in the focal adhesions and lower levels of alpha-1 integrin subunit are expressed at their surface. Although the cytoskeletal and adhesion problems do not originate any major change in the cell cycle of siATXN3-depleted cells, cell death is increased in siATXN3 cultures compared to controls. In summary, in this work we show that the absence of ATXN3 leads to an overt cytoskeletal/adhesion defect raising the possibility that this protein may play a role in the cytoskeleton."xsd:string |
| http://purl.uniprot.org/citations/20637808 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.bbamcr.2010.07.004"xsd:string |
| http://purl.uniprot.org/citations/20637808 | http://purl.uniprot.org/core/author | "Ferreira D."xsd:string |
| http://purl.uniprot.org/citations/20637808 | http://purl.uniprot.org/core/author | "Logarinho E."xsd:string |
| http://purl.uniprot.org/citations/20637808 | http://purl.uniprot.org/core/author | "Maciel P."xsd:string |
| http://purl.uniprot.org/citations/20637808 | http://purl.uniprot.org/core/author | "Rodrigues A.J."xsd:string |
| http://purl.uniprot.org/citations/20637808 | http://purl.uniprot.org/core/author | "Silva T.L."xsd:string |
| http://purl.uniprot.org/citations/20637808 | http://purl.uniprot.org/core/author | "Bajanca F."xsd:string |
| http://purl.uniprot.org/citations/20637808 | http://purl.uniprot.org/core/author | "do Carmo Costa M."xsd:string |
| http://purl.uniprot.org/citations/20637808 | http://purl.uniprot.org/core/date | "2010"xsd:gYear |
| http://purl.uniprot.org/citations/20637808 | http://purl.uniprot.org/core/name | "Biochim Biophys Acta"xsd:string |
| http://purl.uniprot.org/citations/20637808 | http://purl.uniprot.org/core/pages | "1154-1163"xsd:string |
| http://purl.uniprot.org/citations/20637808 | http://purl.uniprot.org/core/title | "Absence of ataxin-3 leads to cytoskeletal disorganization and increased cell death."xsd:string |
| http://purl.uniprot.org/citations/20637808 | http://purl.uniprot.org/core/volume | "1803"xsd:string |
| http://purl.uniprot.org/citations/20637808 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/20637808 |
| http://purl.uniprot.org/citations/20637808 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/20637808 |
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