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dc.contributor.authorAmorim-Silva, Vitor
dc.contributor.authorGarcía-Moreno, Álvaro
dc.contributor.authorLakhssassi, Naoufal
dc.contributor.authorEsteban, Alicia
dc.contributor.authorRosado, Abel
dc.contributor.authorPérez-Sancho, Jessica
dc.contributor.authorLi, Yansha
dc.contributor.authorCastillo, Araceli
dc.contributor.authorPerez-Rodriguez, Josefa 
dc.contributor.authorValpuesta-Fernandez, Victoriano 
dc.contributor.authorZipfel, Cyril
dc.contributor.authorMacho, Alberto
dc.contributor.authorBotella-Mesa, Miguel Angel 
dc.date.accessioned2017-06-23T10:09:43Z
dc.date.available2017-06-23T10:09:43Z
dc.date.created2017
dc.date.issued2017-06-23
dc.identifier.urihttp://hdl.handle.net/10630/13984
dc.descriptionEs una comunicación a un Congreso Internacional de primera línea en el campo objeto de la Tesis Doctoral de Álvaro García
dc.description.abstractBrassinosteroids (BRs) is a group of steroidal hormones that play critical roles in multiple aspects of plant growth and development. BR stimulation at the PM receptors initiates a series of phosphorylation events enabling the nuclear accumulation and activity of the key transcription factor BZR1 and BES1. Previous studies have shown that all BR components associate form an interconnected signaling pathway, although it is not known how these proteins are brought together for the prompt signal transduction upon BR perception. Here we report that plant-specific Tetratricopeptide Thioredoxin-Like TTL proteins are positive regulators of BR signaling functioning as a scaffold of the BR pathway in Arabidopsis. TTL3 interacts with most core components involved in transducing BR signaling, BRI1, BSK1, and BIN2 kinases, the BSU1 phosphatase and the transcription factors BZR1 and BES1. Consistent with this role in BR signaling, mutations in TTL1, TTL2, and TT4 genes cause reduced BR responses, defects that are highly enhanced in a triple ttl1/ttl3/ttl4 mutant. We also show that a functional TTL3-green fluorescence protein is mainly localized in the cytoplasm and that BR treatment increases the association to the plasma membrane. We also show that the cytoplasmic/plasma membrane localization of a functional TTL3-green fluorescence protein is dependent on BR. We propose a novel mechanistic model for optimized BR signaling, in which cytoplasmic/nuclear BR components bound to TTL proteins are translocated to the plasma membrane upon BR perception, which in turn allow the assembly of a BR signaling complex with the goal of ensuring TF de-phosphorylation and nuclear accumulation of the transcription factors.es_ES
dc.description.sponsorshipUniversidad de Málaga. Campus de Excelencia Internacional Andalucía Tech. This work was supported by grants from: (1) Ministerio de Ciencia e Innovación AGL2013-48913-C2-2-R and BIO2014-55380-R; (2) Ministerio de Economía, Industria y Competitividad (BES-2015-071256)es_ES
dc.language.isospaes_ES
dc.rightsinfo:eu-repo/semantics/openAccesses_ES
dc.subjectHormonas vegetaleses_ES
dc.subject.otherAbiotic stresses_ES
dc.subject.otherBrassinoesteroidses_ES
dc.subject.otherArabidopsises_ES
dc.subject.otherScaffoldes_ES
dc.titleScaffold-mediated Assembly of the Brassinosteroid Signaling Components by TTL proteinses_ES
dc.title.alternativeEnsamblaje de componentes de señalización de brasinoesteroides por las proteínas TTLes_ES
dc.typeinfo:eu-repo/semantics/conferenceObjectes_ES
dc.centroFacultad de Cienciases_ES
dc.relation.eventtitleAt the Forefront of Plant Researches_ES
dc.relation.eventplaceGhent, Belgiumes_ES
dc.relation.eventdate15-6-2017es_ES
dc.identifier.orcidhttp://orcid.org/0000-0002-8867-1831es_ES
dc.cclicenseby-nc-ndes_ES


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