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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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author Rodrigues, Ana João
author2 Carvalho, Andreia Alexandra Neves
Ferro, Anabela
Rokka, Anne
Corthals, Garry
Logarinho, Elsa
Maciel, P.
author2_role author
author
author
author
author
author
author_facet Rodrigues, Ana João
Carvalho, Andreia Alexandra Neves
Ferro, Anabela
Rokka, Anne
Corthals, Garry
Logarinho, Elsa
Maciel, P.
author_role author
contributor_name_str_mv RepositóriUM - Universidade do Minho
country_str PT
creators_json_txt [{\"Person.name\":\"Rodrigues, Ana João\"},{\"Person.name\":\"Carvalho, Andreia Alexandra Neves\"},{\"Person.name\":\"Ferro, Anabela\"},{\"Person.name\":\"Rokka, Anne\"},{\"Person.name\":\"Corthals, Garry\"},{\"Person.name\":\"Logarinho, Elsa\"},{\"Person.name\":\"Maciel, P.\"}]
datacite.contributors.contributor.contributorName.fl_str_mv RepositóriUM - Universidade do Minho
datacite.creators.creator.creatorName.fl_str_mv Rodrigues, Ana João
Carvalho, Andreia Alexandra Neves
Ferro, Anabela
Rokka, Anne
Corthals, Garry
Logarinho, Elsa
Maciel, P.
datacite.date.Accepted.fl_str_mv 2009-09-01T00:00:00Z
datacite.date.embargoed.fl_str_mv 10000-01-01T00:00:00Z
datacite.rights.fl_str_mv http://purl.org/coar/access_right/c_16ec
datacite.subjects.subject.fl_str_mv 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
datacite.titles.title.fl_str_mv ATX-3, CDC-48 and UBXN-5: a new trimolecular complex in Caenorhabditis elegans
dc.contributor.none.fl_str_mv RepositóriUM - Universidade do Minho
dc.creator.none.fl_str_mv Rodrigues, Ana João
Carvalho, Andreia Alexandra Neves
Ferro, Anabela
Rokka, Anne
Corthals, Garry
Logarinho, Elsa
Maciel, P.
dc.date.Accepted.fl_str_mv 2009-09-01T00:00:00Z
dc.date.embargoed.fl_str_mv 10000-01-01T00:00:00Z
dc.format.none.fl_str_mv application/pdf
dc.identifier.none.fl_str_mv https://hdl.handle.net/1822/67644
dc.language.none.fl_str_mv eng
dc.publisher.none.fl_str_mv Elsevier
dc.rights.none.fl_str_mv http://purl.org/coar/access_right/c_16ec
dc.subject.none.fl_str_mv 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
dc.title.fl_str_mv ATX-3, CDC-48 and UBXN-5: a new trimolecular complex in Caenorhabditis elegans
dc.type.none.fl_str_mv http://purl.org/coar/resource_type/c_6501
description 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.
dirty 0
eu_rights_str_mv restrictedAccess
format article
fulltext.url.fl_str_mv https://repositorium.uminho.pt/bitstreams/3e3d8092-0214-4dbe-8045-fcc0906799fc/download
id rum_c0058cd00ca2ef8d495cfe5b653de6a8
identifier.url.fl_str_mv https://hdl.handle.net/1822/67644
instacron_str repositorium
institution Universidade do Minho
instname_str Universidade do Minho
language eng
network_acronym_str rum
network_name_str RepositóriUM - Universidade do Minho
oai_identifier_str oai:repositorium.uminho.pt:1822/67644
organization_str_mv urn:organizationAcronym:repositorium
person_str_mv Rodrigues, Ana João
Carvalho, Andreia Alexandra Neves
Ferro, Anabela
Rokka, Anne
Corthals, Garry
Logarinho, Elsa
Maciel, P.
publishDate 2009
publisher.none.fl_str_mv Elsevier
reponame_str RepositóriUM - Universidade do Minho
repository_id_str urn:repositoryAcronym:rum
service_str_mv urn:repositoryAcronym:rum
spelling engElsevierporAtaxin-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.application/pdfporATX-3, CDC-48 and UBXN-5: a new trimolecular complex in Caenorhabditis elegansRodrigues, Ana JoãoCarvalho, Andreia Alexandra NevesFerro, AnabelaRokka, AnneCorthals, GarryLogarinho, ElsaMaciel, P.HostingInstitutionOrganizationalRepositóriUM - Universidade do Minhoe-mailmailto:repositorium@usdb.uminho.ptrepositorium@usdb.uminho.ptPMID19545544ISSNIsPartOf0006-291XEISSNIsPartOf1090-2104DOIIsPartOf10.1016/j.bbrc.2009.06.0922009-092009-09-01T00:00:00Z10000-01-01T00:00:00ZHandlehttps://hdl.handle.net/1822/67644http://purl.org/coar/access_right/c_16ecrestricted accessAdaptor proteins, Signal transducingAdenosine triphosphatasesAnimalsAtaxin-3Caenorhabditis elegansCaenorhabditis elegans proteinsCell cycle proteinsMultiprotein complexesNerve tissue proteinsProtein interaction domains and motifsProtein interaction mappingValosin containing proteinPolyglutamineMachado–Joseph diseaseSpinocerebellar ataxia type 3Ubiquitin–proteasome pathwayDeubiquitylating enzyme1550519 bytesliteraturehttp://purl.org/coar/resource_type/c_6501journal articlehttp://purl.org/coar/access_right/c_f1cfapplication/pdffulltexthttps://repositorium.uminho.pt/bitstreams/3e3d8092-0214-4dbe-8045-fcc0906799fc/download
spellingShingle ATX-3, CDC-48 and UBXN-5: a new trimolecular complex in Caenorhabditis elegans
Rodrigues, Ana João
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
status SINGLETON
subject.fl_str_mv 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
title ATX-3, CDC-48 and UBXN-5: a new trimolecular complex in Caenorhabditis elegans
title_full ATX-3, CDC-48 and UBXN-5: a new trimolecular complex in Caenorhabditis elegans
title_fullStr ATX-3, CDC-48 and UBXN-5: a new trimolecular complex in Caenorhabditis elegans
title_full_unstemmed ATX-3, CDC-48 and UBXN-5: a new trimolecular complex in Caenorhabditis elegans
title_short ATX-3, CDC-48 and UBXN-5: a new trimolecular complex in Caenorhabditis elegans
title_sort ATX-3, CDC-48 and UBXN-5: a new trimolecular complex in Caenorhabditis elegans
topic 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
topic_facet 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
url https://hdl.handle.net/1822/67644
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