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dc.contributor.authorQuintero, Francisco J.
dc.contributor.authorMartínez-Atienza, Juliana
dc.contributor.authorVillalta, Irene
dc.contributor.authorJiang, Xingyu
dc.contributor.authorKim, Woeyeon
dc.contributor.authorAli, Zhair
dc.contributor.authorFujii, Hiroaki
dc.contributor.authorMendoza, Imelda
dc.contributor.authorYun, Daejin
dc.contributor.authorZhu, Jian-Kang
dc.contributor.authorPardo, José Manuel
dc.date.accessioned2015-08-03T09:02:44Z
dc.date.available2015-08-03T09:02:44Z
dc.date.issued2011-01-24
dc.identifier.citationQuintero, F. J., Martinez-Atienza, J., Villalta, I., Jiang, X., Kim, W.-Y., Ali, Z., … Pardo, J. M. (2011). Activation of the plasma membrane Na/H antiporter Salt-Overly-Sensitive 1 (SOS1) by phosphorylation of an auto-inhibitory C-terminal domain. Proceedings of the National Academy of Sciences, 108(6), 2611–2616. doi:10.1073/pnas.1018921108
dc.identifier.issn00278424
dc.identifier.pmid21262798
dc.identifier.doi10.1073/pnas.1018921108
dc.identifier.urihttp://hdl.handle.net/10754/561705
dc.description.abstractThe plasma membrane sodium/proton exchanger Salt-Overly-Sensitive 1 (SOS1) is a critical salt tolerance determinant in plants. The SOS2-SOS3 calcium-dependent protein kinase complex upregulates SOS1 activity, but the mechanistic details of this crucial event remain unresolved. Here we show that SOS1 is maintained in a resting state by a C-terminal auto-inhibitory domain that is the target of SOS2-SOS3. The auto-inhibitory domain interacts intramolecularly with an adjacent domain of SOS1 that is essential for activity. SOS1 is relieved from auto-inhibition upon phosphorylation of the auto-inhibitory domain by SOS2-SOS3. Mutation of the SOS2 phosphorylation and recognition site impeded the activation of SOS1 in vivo and in vitro. Additional amino acid residues critically important for SOS1 activity and regulation were identified in a genetic screen for hypermorphic alleles.
dc.description.sponsorshipWe are indebted to Unidad de Proteomica, Centro Nacional de Investigaciones Cardiovasculares Carlos III, for mass-spectrometric analysis. This work was supported by Grants BIO2009-08641 and CSD2007-00057 from the Ministerio de Ciencia e Innovacion (cofinanced by Fondo Europeo de Desarrollo Regional) (to J.M.P. and F.J.Q.), World Class University Program Grant R32-10148 (to D.-J.Y. and W.Y.K.), and National Institutes of Health Grants R01GM070795 and R01GM059138 (to J.-K.Z.).
dc.publisherProceedings of the National Academy of Sciences
dc.relation.urlhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC3038701
dc.subjectIon transport
dc.subjectSalinity
dc.subjectSodium tolerance
dc.titleActivation of the plasma membrane Na/H antiporter salt-overly-sensitive 1 (SOS1) by phosphorylation of an auto-inhibitory C-terminal domain
dc.typeArticle
dc.contributor.departmentDesert Agriculture Initiative
dc.contributor.departmentBiological and Environmental Sciences and Engineering (BESE) Division
dc.identifier.journalProceedings of the National Academy of Sciences
dc.identifier.pmcidPMC3038701
dc.contributor.institutionInstituto de Recursos Naturales Y Agrobiologia, Consejo Superior de Investigaciones Cientificas, 41012 Sevilla, Spain
dc.contributor.institutionDivision of Applied Life Science (BK21 Program), Plant Molecular Biology and Biotechnology Research Center, Graduate School of Gyeongsang National University, Jinju 660-701, South Korea
dc.contributor.institutionDepartment of Horticulture and Landscape Architecture, Purdue University, West Lafayette, IN 47907, United States
kaust.personFujii, Hiroaki
kaust.personZhu, Jian-Kang
kaust.personPardo, José Manuel
dc.date.published-online2011-01-24
dc.date.published-print2011-02-08


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