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ATX-3, CDC-48 and UBXN-5: a new trimolecular complex in Caenorhabditis elegans

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Resumo: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.
Autores principais:Rodrigues, Ana João
Outros Autores:Carvalho, Andreia Alexandra Neves; Ferro, Anabela; Rokka, Anne; Corthals, Garry; Logarinho, Elsa; Maciel, P.
Assunto:Adaptor proteins, Signal transducing Adenosine triphosphatases Animals Ataxin-3 Caenorhabditis elegans Caenorhabditis elegans proteins Cell cycle proteins Multiprotein complexes Nerve tissue proteins Protein interaction domains and motifs Protein interaction mapping Valosin containing protein Polyglutamine Machado–Joseph disease Spinocerebellar ataxia type 3 Ubiquitin–proteasome pathway Deubiquitylating enzyme
Ano:2009
País:Portugal
Tipo de documento:artigo
Tipo de acesso:acesso restrito
Instituição associada:Universidade do Minho
Idioma:inglês
Origem:RepositóriUM - Universidade do Minho

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