Activation of the plasma membrane Na/H antiporter salt-overly-sensitive 1 (SOS1) by phosphorylation of an auto-inhibitory C-terminal domain
AuthorsQuintero, Francisco J.
Pardo, José Manuel
KAUST DepartmentBiological and Environmental Science and Engineering (BESE) Division
Center for Desert Agriculture
Online Publication Date2011-01-24
Print Publication Date2011-02-08
Permanent link to this recordhttp://hdl.handle.net/10754/561705
MetadataShow full item record
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.
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
SponsorsWe 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.).
PubMed Central IDPMC3038701
- Transgenic evaluation of activated mutant alleles of SOS2 reveals a critical requirement for its kinase activity and C-terminal regulatory domain for salt tolerance in Arabidopsis thaliana.
- Authors: Guo Y, Qiu QS, Quintero FJ, Pardo JM, Ohta M, Zhang C, Schumaker KS, Zhu JK
- Issue date: 2004 Feb
- The protein kinase complex CBL10-CIPK8-SOS1 functions in Arabidopsis to regulate salt tolerance.
- Authors: Yin X, Xia Y, Xie Q, Cao Y, Wang Z, Hao G, Song J, Zhou Y, Jiang X
- Issue date: 2020 Mar 25
- Regulation of SOS1, a plasma membrane Na+/H+ exchanger in Arabidopsis thaliana, by SOS2 and SOS3.
- Authors: Qiu QS, Guo Y, Dietrich MA, Schumaker KS, Zhu JK
- Issue date: 2002 Jun 11
- Regulation of vacuolar Na+/H+ exchange in Arabidopsis thaliana by the salt-overly-sensitive (SOS) pathway.
- Authors: Qiu QS, Guo Y, Quintero FJ, Pardo JM, Schumaker KS, Zhu JK
- Issue date: 2004 Jan 2
- 14-3-3 Proteins and Other Candidates form Protein-Protein Interactions with the Cytosolic C-terminal End of SOS1 Affecting Its Transport Activity.
- Authors: Duscha K, Martins Rodrigues C, Müller M, Wartenberg R, Fliegel L, Deitmer JW, Jung M, Zimmermann R, Neuhaus HE
- Issue date: 2020 May 8