Activation of the plasma membrane Na/H antiporter salt-overly-sensitive 1 (SOS1) by phosphorylation of an auto-inhibitory C-terminal domain

Handle URI:
http://hdl.handle.net/10754/561705
Title:
Activation of the plasma membrane Na/H antiporter salt-overly-sensitive 1 (SOS1) by phosphorylation of an auto-inhibitory C-terminal domain
Authors:
Quintero, Francisco J.; Martínez-Atienza, Juliana; Villalta, Irene; Jiang, Xingyu; Kim, Woeyeon; Ali, Zhair; Fujii, Hiroaki ( 0000-0002-0013-5891 ) ; Mendoza, Imelda; Yun, Daejin; Zhu, Jian-Kang; Pardo, José Manuel
Abstract:
The 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.
KAUST Department:
Center for Desert Agriculture
Publisher:
Proceedings of the National Academy of Sciences
Journal:
Proceedings of the National Academy of Sciences
Issue Date:
24-Jan-2011
DOI:
10.1073/pnas.1018921108
PubMed ID:
21262798
PubMed Central ID:
PMC3038701
Type:
Article
ISSN:
00278424
Sponsors:
We 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.).
Additional Links:
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3038701
Appears in Collections:
Articles; Center for Desert Agriculture

Full metadata record

DC FieldValue Language
dc.contributor.authorQuintero, Francisco J.en
dc.contributor.authorMartínez-Atienza, Julianaen
dc.contributor.authorVillalta, Ireneen
dc.contributor.authorJiang, Xingyuen
dc.contributor.authorKim, Woeyeonen
dc.contributor.authorAli, Zhairen
dc.contributor.authorFujii, Hiroakien
dc.contributor.authorMendoza, Imeldaen
dc.contributor.authorYun, Daejinen
dc.contributor.authorZhu, Jian-Kangen
dc.contributor.authorPardo, José Manuelen
dc.date.accessioned2015-08-03T09:02:44Zen
dc.date.available2015-08-03T09:02:44Zen
dc.date.issued2011-01-24en
dc.identifier.issn00278424en
dc.identifier.pmid21262798en
dc.identifier.doi10.1073/pnas.1018921108en
dc.identifier.urihttp://hdl.handle.net/10754/561705en
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.en
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.).en
dc.publisherProceedings of the National Academy of Sciencesen
dc.relation.urlhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC3038701en
dc.subjectIon transporten
dc.subjectSalinityen
dc.subjectSodium toleranceen
dc.titleActivation of the plasma membrane Na/H antiporter salt-overly-sensitive 1 (SOS1) by phosphorylation of an auto-inhibitory C-terminal domainen
dc.typeArticleen
dc.contributor.departmentCenter for Desert Agricultureen
dc.identifier.journalProceedings of the National Academy of Sciencesen
dc.identifier.pmcidPMC3038701en
dc.contributor.institutionInstituto de Recursos Naturales Y Agrobiologia, Consejo Superior de Investigaciones Cientificas, 41012 Sevilla, Spainen
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 Koreaen
dc.contributor.institutionDepartment of Horticulture and Landscape Architecture, Purdue University, West Lafayette, IN 47907, United Statesen
kaust.authorFujii, Hiroakien
kaust.authorZhu, Jian-Kangen
kaust.authorPardo, José Manuelen

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