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

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    Type
    Article
    Authors
    Quintero, Francisco J.
    Martínez-Atienza, Juliana
    Villalta, Irene
    Jiang, Xingyu
    Kim, Woeyeon
    Ali, Zhair
    Fujii, Hiroaki cc
    Mendoza, Imelda
    Yun, Daejin
    Zhu, Jian-Kang cc
    Pardo, José Manuel
    KAUST Department
    Biological and Environmental Science and Engineering (BESE) Division
    Center for Desert Agriculture
    Date
    2011-01-24
    Online Publication Date
    2011-01-24
    Print Publication Date
    2011-02-08
    Permanent link to this record
    http://hdl.handle.net/10754/561705
    
    Metadata
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    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.
    Citation
    Quintero, 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
    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.).
    Publisher
    Proceedings of the National Academy of Sciences
    Journal
    Proceedings of the National Academy of Sciences
    DOI
    10.1073/pnas.1018921108
    PubMed ID
    21262798
    PubMed Central ID
    PMC3038701
    Additional Links
    http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3038701
    ae974a485f413a2113503eed53cd6c53
    10.1073/pnas.1018921108
    Scopus Count
    Collections
    Articles; Biological and Environmental Science and Engineering (BESE) Division; Center for Desert Agriculture

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