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dc.contributor.authorPuerta Turrillas, María Luisa de la 
dc.contributor.authorTrinidad, Antonio G.
dc.contributor.authorRodríguez, María del Carmen
dc.contributor.authorBogetz, Jori
dc.contributor.authorSánchez Crespo, Mariano
dc.contributor.authorMustelin, Tomas
dc.contributor.authorAlonso, Andrés
dc.contributor.authorBayón Prieto, Yolanda 
dc.date.accessioned2021-07-19T05:40:23Z
dc.date.available2021-07-19T05:40:23Z
dc.date.issued2009
dc.identifier.citationPLoS ONE, 2009, vol. 4, n. 2, p. e4431es
dc.identifier.issn1932-6203es
dc.identifier.urihttps://uvadoc.uva.es/handle/10324/47496
dc.descriptionProducción Científicaes
dc.description.abstractYopH is an exceptionally active tyrosine phosphatase that is essential for virulence of Yersinia pestis, the bacterium causing plague. YopH breaks down signal transduction mechanisms in immune cells and inhibits the immune response. Only a few substrates for YopH have been characterized so far, for instance p130Cas and Fyb, but in view of YopH potency and the great number of proteins involved in signalling pathways it is quite likely that more proteins are substrates of this phosphatase. In this respect, we show here YopH interaction with several proteins not shown before, such as Gab1, Gab2, p85, and Vav and analyse the domains of YopH involved in these interactions. Furthermore, we show that Gab1, Gab2 and Vav are not dephosphorylated by YopH, in contrast to Fyb, Lck, or p85, which are readily dephosphorylated by the phosphatase. These data suggests that YopH might exert its actions by interacting with adaptors involved in signal transduction pathways, what allows the phosphatase to reach and dephosphorylate its susbstrates.es
dc.format.mimetypeapplication/pdfes
dc.language.isoenges
dc.publisherPublic Library of Sciencees
dc.rights.accessRightsinfo:eu-repo/semantics/openAccesses
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/*
dc.subject.classificationBacteriases
dc.subject.classificationYersiniaes
dc.subject.classificationTyrosine Phosphatasees
dc.titleCharacterization of new substrates targeted by yersinia tyrosine phosphatase YopHes
dc.typeinfo:eu-repo/semantics/articlees
dc.rights.holder© Public Library of Sciencees
dc.identifier.doi10.1371/journal.pone.0004431es
dc.relation.publisherversionhttps://journals.plos.org/plosone/article?id=10.1371/journal.pone.0004431es
dc.identifier.publicationfirstpagee4431es
dc.identifier.publicationissue2es
dc.identifier.publicationtitlePLoS ONEes
dc.identifier.publicationvolume4es
dc.peerreviewedSIes
dc.description.projectJunta de Castilla y León (VA002B05)
dc.description.projectPlan Nacional de Biología Fundamental (grant BFU2006-01203/BMC)
dc.identifier.essn1932-6203es
dc.rightsAttribution-NonCommercial-NoDerivatives 4.0 Internacional*
dc.type.hasVersioninfo:eu-repo/semantics/publishedVersiones
dc.subject.unesco24 Ciencias de la Vidaes


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