Utilize este identificador para referenciar este registo:
https://hdl.handle.net/1822/67644
Registo completo
Campo DC | Valor | Idioma |
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dc.contributor.author | Rodrigues, Ana João | por |
dc.contributor.author | Carvalho, Andreia Alexandra Neves | por |
dc.contributor.author | Ferro, Anabela | por |
dc.contributor.author | Rokka, Anne | por |
dc.contributor.author | Corthals, Garry | por |
dc.contributor.author | Logarinho, Elsa | por |
dc.contributor.author | Maciel, P. | por |
dc.date.accessioned | 2020-10-22T14:01:51Z | - |
dc.date.issued | 2009-09 | - |
dc.identifier.issn | 0006-291X | - |
dc.identifier.uri | https://hdl.handle.net/1822/67644 | - |
dc.description.abstract | Ataxin-3 is the protein involved in Machado-Joseph disease, a neurodegenerative disorder caused by a polyglutamine expansion. Ataxin-3 binds ubiquitylated proteins and acts as a deubiquitylating enzyme in vitro. It was previously proposed that ataxin-3, along with the VCP/p97 protein, escorts ubiquitylated substrates for proteasomal degradation, although other players of this escort complex were not identified yet. In this work, we show that the Caenorhabditis elegans ataxin-3 protein (ATX-3) interacts with both VCP/p97 worm homologs, CDC-48.1 and CDC-48.2 and we map the interaction domains. We describe a motility defect in both ATX-3 and CDC-48.1 mutants and, in addition, we identify a new protein interactor, UBXN-5, potentially an adaptor of the CDC-48-ATX-3 escort complex. CDC-48 binds to both ATX-3 and UBXN-5 in a non-competitive manner, suggesting the formation of a trimolecular complex. Both CDC-48 and ATX-3, but not UBXN-5, were able to bind K-48 polyubiquitin chains, the standard signal for proteasomal degradation. Additionally, we describe several common interactors of ATX-3 and UBXN-5, some of which can be in vivo targets of this complex. | por |
dc.description.sponsorship | Authors thank Caenorhabditis Genetics Center (CGC). A.J.R.thanks all the PM group members for helpful discussions, espe-cially A. Teixeira-Castro. A special recognition to T. Hoppe for pro-viding the double mutant strains. This research was supported byFEDER/FCT (POCTI/SAU-MMO/60412/2004), Portuguese-AmericanFoundation for Development (FLAD), and National Ataxia Founda-tion (NAF). AJ.R. and A.F. received FCT scholarships. | por |
dc.language.iso | eng | por |
dc.publisher | Elsevier | por |
dc.relation | info:eu-repo/grantAgreement/FCT/POCI/60412/PT | por |
dc.rights | closedAccess | por |
dc.subject | Adaptor proteins, Signal transducing | por |
dc.subject | Adenosine triphosphatases | por |
dc.subject | Animals | por |
dc.subject | Ataxin-3 | por |
dc.subject | Caenorhabditis elegans | por |
dc.subject | Caenorhabditis elegans proteins | por |
dc.subject | Cell cycle proteins | por |
dc.subject | Multiprotein complexes | por |
dc.subject | Nerve tissue proteins | por |
dc.subject | Protein interaction domains and motifs | por |
dc.subject | Protein interaction mapping | por |
dc.subject | Valosin containing protein | por |
dc.subject | Polyglutamine | por |
dc.subject | Machado–Joseph disease | por |
dc.subject | Spinocerebellar ataxia type 3 | por |
dc.subject | Ubiquitin–proteasome pathway | por |
dc.subject | Deubiquitylating enzyme | por |
dc.title | ATX-3, CDC-48 and UBXN-5: a new trimolecular complex in Caenorhabditis elegans | por |
dc.type | article | por |
dc.peerreviewed | yes | por |
dc.relation.publisherversion | https://www.sciencedirect.com/science/article/pii/S0006291X09011991 | por |
oaire.citationStartPage | 575 | por |
oaire.citationEndPage | 581 | por |
oaire.citationIssue | 4 | por |
oaire.citationVolume | 386 | por |
dc.identifier.eissn | 1090-2104 | - |
dc.identifier.doi | 10.1016/j.bbrc.2009.06.092 | por |
dc.date.embargo | 10000-01-01 | - |
dc.identifier.pmid | 19545544 | por |
dc.subject.wos | Science & Technology | por |
sdum.journal | Biochemical and Biophysical Research Communications | por |
Aparece nas coleções: | ICVS - Artigos em revistas internacionais / Papers in international journals |
Ficheiros deste registo:
Ficheiro | Descrição | Tamanho | Formato | |
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rodrigues2009.pdf Acesso restrito! | 1,51 MB | Adobe PDF | Ver/Abrir |