Utilize este identificador para referenciar este registo: http://hdl.handle.net/10400.7/863
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dc.contributor.authorCarvalho, Raquel F.-
dc.contributor.authorSzakonyi, Dóra-
dc.contributor.authorSimpson, Craig G.-
dc.contributor.authorBarbosa, Inês C.R.-
dc.contributor.authorBrown, John W.S.-
dc.contributor.authorBaena-González, Elena-
dc.contributor.authorDuque, Paula-
dc.date.accessioned2018-04-13T11:02:07Z-
dc.date.available2018-04-13T11:02:07Z-
dc.date.issued2016-08-
dc.identifier.citationRaquel F. Carvalho, Dóra Szakonyi, Craig G. Simpson, Inês C.R. Barbosa, John W.S. Brown, Elena Baena-González, Paula Duque (2018). The Arabidopsis SR45 Splicing Factor, a Negative Regulator of Sugar Signaling, Modulates SNF1-Related Protein Kinase 1 Stability. Plant Cell. 28(8):1910-25. doi: 10.1105/tpc.16.00301pt_PT
dc.identifier.urihttp://hdl.handle.net/10400.7/863-
dc.descriptionThe deposited article is a post-print version and has been submitted to peer review.pt_PT
dc.descriptionThis publication hasn't any creative commons license associated.pt_PT
dc.descriptionThis deposit is composed by the main article, and it hasn't any supplementary materials associated.pt_PT
dc.description.abstractThe ability to sense and respond to sugar signals allows plants to cope with environmental and metabolic changes by adjusting growth and development accordingly. We previously reported that the SR45 splicing factor negatively regulates glucose signaling during early seedling development in Arabidopsis thaliana Here, we show that under glucose-fed conditions, the Arabidopsis sr45-1 loss-of-function mutant contains higher amounts of the energy-sensing SNF1-Related Protein Kinase 1 (SnRK1) despite unaffected SnRK1 transcript levels. In agreement, marker genes for SnRK1 activity are upregulated in sr45-1 plants, and the glucose hypersensitivity of sr45-1 is attenuated by disruption of the SnRK1 gene. Using a high-resolution RT-PCR panel, we found that the sr45-1 mutation broadly targets alternative splicing in vivo, including that of the SR45 pre-mRNA itself. Importantly, the enhanced SnRK1 levels in sr45-1 are suppressed by a proteasome inhibitor, indicating that SR45 promotes targeting of the SnRK1 protein for proteasomal destruction. Finally, we demonstrate that SR45 regulates alternative splicing of the Arabidopsis 5PTase13 gene, which encodes an inositol polyphosphate 5-phosphatase previously shown to interact with and regulate the stability of SnRK1 in vitro, thus providing a mechanistic link between SR45 function and the modulation of degradation of the SnRK1 energy sensor in response to sugars.pt_PT
dc.description.sponsorshipFundação para a Ciência e a Tecnologia grants: (PTDC/BIA-PLA/3937/2012, PTDC/BIA-PLA/1084/2014, SFRH/BPD/80073/2011, SFRH/BPD/94796/2013); EMBO Installation Program: (EMBO-Proj.1984); Scottish Government Rural and Environment Science and Analytical Services (RESAS).pt_PT
dc.language.isoengpt_PT
dc.publisherAmerican Society of Plant Biologistspt_PT
dc.relationinfo:eu-repo/grantAgreement/FCT/3599-PPCDT/130540/PTpt_PT
dc.relationPTDC/BIA-PLA/1084/2014pt_PT
dc.relationinfo:eu-repo/grantAgreement/FCT/SFRH/SFRH%2FBPD%2F80073%2F2011/PTpt_PT
dc.relationSFRH/BPD/94796/2013pt_PT
dc.relationEMBO-Proj.1984pt_PT
dc.rightsopenAccesspt_PT
dc.subjectAlternative Splicingpt_PT
dc.subjectArabidopsispt_PT
dc.subjectArabidopsis Proteinspt_PT
dc.subjectPhosphoric Monoester Hydrolasespt_PT
dc.subjectProtein Stabilitypt_PT
dc.subjectProtein-Serine-Threonine Kinasespt_PT
dc.subjectRNA-Binding Proteinspt_PT
dc.subjectReverse Transcriptase Polymerase Chain Reactionpt_PT
dc.titleThe Arabidopsis SR45 Splicing Factor, a Negative Regulator of Sugar Signaling, Modulates SNF1-Related Protein Kinase 1 Stabilitypt_PT
dc.typearticlept_PT
dc.description.versioninfo:eu-repo/semantics/publishedVersionpt_PT
degois.publication.firstPage1910pt_PT
degois.publication.issue8pt_PT
degois.publication.lastPage1925pt_PT
degois.publication.titlePlant Cellpt_PT
dc.relation.publisherversionhttp://www.plantcell.org/content/28/8/1910.longpt_PT
dc.peerreviewedyespt_PT
degois.publication.volume28pt_PT
dc.identifier.doi10.1105/tpc.16.00301pt_PT
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