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An N-terminal SIAH-interacting motif regulates the stability of the ubiquitin specific protease (USP)-19

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dc.creatorVelasco, Kellyspa
dc.creatorZhao, Binspa
dc.creatorCallegari, Simonespa
dc.creatorAltun, Mikaelspa
dc.creatorLiu, Haiyinspa
dc.creatorHassink, Gercospa
dc.creatorMasucci, Maria G.spa
dc.creatorLindsten, Kristinaspa
dc.date.accessioned2020-05-26T00:02:40Z
dc.date.available2020-05-26T00:02:40Z
dc.date.created2013spa
dc.description.abstractThe Ubiquitin Specific Protease-19 (USP19) regulates cell cycle progression and is involved in the cellular response to different types of stress, including the unfolded protein response (UPR), hypoxia and muscle atrophy. Using the unique N-terminal domain as bait in a yeast-two hybrid screen we have identified the ubiquitin ligases Seven In Absentia Homolog (SIAH)-1 and SIAH2 as binding partners of USP19. The interaction is mediated by a SIAH-consensus binding motif and promotes USP19 ubiquitylation and proteasome-dependent degradation. These findings identify USP19 as a common substrate of the SIAH ubiquitin ligases. © 2013 Elsevier Inc.eng
dc.format.mimetypeapplication/pdf
dc.identifier.doihttps://doi.org/10.1016/j.bbrc.2013.02.094
dc.identifier.issn0006291X
dc.identifier.issn10902104
dc.identifier.urihttps://repository.urosario.edu.co/handle/10336/23513
dc.language.isoengspa
dc.relation.citationEndPage395
dc.relation.citationIssueNo. 4
dc.relation.citationStartPage390
dc.relation.citationTitleBiochemical and Biophysical Research Communications
dc.relation.citationVolumeVol. 433
dc.relation.ispartofBiochemical and Biophysical Research Communications, ISSN:0006291X, 10902104, Vol.433, No.4 (2013); pp. 390-395spa
dc.relation.urihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-84876466143&doi=10.1016%2fj.bbrc.2013.02.094&partnerID=40&md5=0ca1e002ffdb2976fa31c95bc306e043spa
dc.rights.accesRightsinfo:eu-repo/semantics/openAccess
dc.rights.accesoAbierto (Texto Completo)spa
dc.source.instnameinstname:Universidad del Rosariospa
dc.source.reponamereponame:Repositorio Institucional EdocURspa
dc.subject.keywordSeven In Absentia Homolog 1spa
dc.subject.keywordSeven In Absentia Homolog 2spa
dc.subject.keywordUbiquitinspa
dc.subject.keywordUbiquitin specific protease 19spa
dc.subject.keywordUnclassified drugspa
dc.subject.keywordAmino terminal sequencespa
dc.subject.keywordArticlespa
dc.subject.keywordHumanspa
dc.subject.keywordHuman cellspa
dc.subject.keywordPriority journalspa
dc.subject.keywordProtein protein interactionspa
dc.subject.keywordProtein stabilityspa
dc.subject.keywordUbiquitinationspa
dc.subject.keywordUnfolded protein responsespa
dc.subject.keywordAmino Acid Motifsspa
dc.subject.keywordBlottingeng
dc.subject.keywordComputational Biologyspa
dc.subject.keywordEndopeptidasesspa
dc.subject.keywordEnzyme Stabilityspa
dc.subject.keywordHEK293 Cellsspa
dc.subject.keywordHela Cellsspa
dc.subject.keywordHumansspa
dc.subject.keywordImmunoprecipitationspa
dc.subject.keywordNuclear Proteinsspa
dc.subject.keywordProteasome Endopeptidase Complexspa
dc.subject.keywordProtein Bindingspa
dc.subject.keywordProtein Interaction Mappingspa
dc.subject.keywordProteolysisspa
dc.subject.keywordTwo-Hybrid System Techniquesspa
dc.subject.keywordUbiquitin-Protein Ligasesspa
dc.subject.keywordUbiquitinationspa
dc.subject.keywordProteasomal degradationspa
dc.subject.keywordSIAH degronspa
dc.subject.keywordSIAH1 ligasespa
dc.subject.keywordUSP19spa
dc.titleAn N-terminal SIAH-interacting motif regulates the stability of the ubiquitin specific protease (USP)-19spa
dc.typearticleeng
dc.type.hasVersioninfo:eu-repo/semantics/publishedVersion
dc.type.spaArtículospa
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