Please use this identifier to cite or link to this item: http://hdl.handle.net/1822/67644

TitleATX-3, CDC-48 and UBXN-5: a new trimolecular complex in Caenorhabditis elegans
Author(s)Rodrigues, Ana João
Carvalho, Andreia Alexandra Neves
Ferro, Anabela
Rokka, Anne
Corthals, Garry
Logarinho, Elsa
Maciel, P.
KeywordsAdaptor 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
Issue dateSep-2009
PublisherElsevier
JournalBiochemical and Biophysical Research Communications
Abstract(s)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.
TypeArticle
URIhttp://hdl.handle.net/1822/67644
DOI10.1016/j.bbrc.2009.06.092
ISSN0006-291X
e-ISSN1090-2104
Publisher versionhttps://www.sciencedirect.com/science/article/pii/S0006291X09011991
Peer-Reviewedyes
AccessRestricted access (Author)
Appears in Collections:ICVS - Artigos em revistas internacionais / Papers in international journals

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