Please use this identifier to cite or link to this item:
https://hdl.handle.net/10316/5324
DC Field | Value | Language |
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dc.contributor.author | Ferro, Anabela | - |
dc.contributor.author | Carvalho, Ana Luísa | - |
dc.contributor.author | Teixeira-Castro, Andreia | - |
dc.contributor.author | Almeida, Carla | - |
dc.contributor.author | Tomé, Ricardo J. | - |
dc.contributor.author | Cortes, Luísa | - |
dc.contributor.author | Rodrigues, Ana-João | - |
dc.contributor.author | Logarinho, Elsa | - |
dc.contributor.author | Sequeiros, Jorge | - |
dc.contributor.author | Macedo-Ribeiro, Sandra | - |
dc.contributor.author | Maciel, Patrícia | - |
dc.date.accessioned | 2008-09-01T15:40:18Z | - |
dc.date.available | 2008-09-01T15:40:18Z | - |
dc.date.issued | 2007 | en_US |
dc.identifier.citation | Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1773:11 (2007) 1619-1627 | en_US |
dc.identifier.uri | https://hdl.handle.net/10316/5324 | - |
dc.description.abstract | Machado-Joseph disease (MJD/SCA3) is an autosomal dominant neurodegenerative disease caused by the expansion of a CAG tract in the coding portion of the ATXN3 gene. The presence of ubiquitin-positive aggregates of the defective protein in affected neurons is characteristic of this and most of the polyglutamine disorders. Recently, the accumulation of the neural precursor cell expressed developmentally downregulated 8 (NEDD8), a ubiquitin-like protein, in the inclusions of MJD brains was reported. Here, we report a new molecular interaction between wild-type ataxin-3 and NEDD8, using in vitro and in situ approaches. Furthermore, we show that this interaction is not dependent on the ubiquitin-interacting motifs in ataxin-3, since the presence of the Josephin domain is sufficient for the interaction to occur. The conservation of the interaction between the Caenorhabditis elegans ataxin-3 homologue (atx-3) and NEDD8 suggests its biological and functional relevance. Molecular docking studies of the NEDD8 molecule to the Josephin domain of ataxin-3 suggest that NEDD8 interacts with ataxin-3 in a substrate-like mode. In agreement, ataxin-3 displays deneddylase activity against a fluorogenic NEDD8 substrate. | en_US |
dc.description.uri | http://www.sciencedirect.com/science/article/B6T20-4PGY4KR-1/1/1fa5da8c83d1c67f4864d0738ff047e3 | en_US |
dc.format.mimetype | aplication/PDF | en |
dc.language.iso | eng | eng |
dc.rights | openAccess | eng |
dc.subject | Polyglutamine | en_US |
dc.subject | Ubiquitin | en_US |
dc.subject | E3 ligase | en_US |
dc.subject | Neurodegeneration | en_US |
dc.subject | MJD/SCA3 | en_US |
dc.title | NEDD8: A new ataxin-3 interactor | en_US |
dc.type | article | en_US |
item.fulltext | Com Texto completo | - |
item.grantfulltext | open | - |
item.languageiso639-1 | en | - |
item.cerifentitytype | Publications | - |
item.openairetype | article | - |
item.openairecristype | http://purl.org/coar/resource_type/c_18cf | - |
crisitem.author.researchunit | CNC - Center for Neuroscience and Cell Biology | - |
crisitem.author.orcid | 0000-0001-8368-6666 | - |
Appears in Collections: | FCTUC Ciências da Vida - Artigos em Revistas Internacionais |
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file8c1ef1afa30f497095d6926f85593f9d.pdf | 909.23 kB | Adobe PDF | View/Open |
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