Skip to main content
Log in

Structural insight into SOS signalling in response to salt stress

  • Research Briefing
  • Published:

From Nature Plants

View current issue Submit your manuscript

The plasma membrane Na+/H+ antiporter SOS1 has a pivotal role in determining salinity tolerance in plants. This study investigates the structure and function of SOS1 from Oryza sativa (rice), elucidating its architecture and activation mechanism, with notable implications for improving crop salt tolerance.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Fig. 1: Working model for SOS1 activation and Na+ transport.

References

  1. Munns, R. & Tester, M. Mechanisms of salinity tolerance. Annu. Rev. Plant Biol. 59, 651–681 (2008). A review article summarizing the physiology and molecular mechanisms in response to salinity stress in plants.

    Article  CAS  PubMed  Google Scholar 

  2. Zhu, J. K. Abiotic stress signalling and responses in plants. Cell 167, 313–324 (2016). A review article that presents the core stress-signalling pathways in plants and their involvement in the regulation of stress response proteins.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  3. Wu, S. J. et al. SOS1, a genetic locus essential for salt tolerance and potassium acquisition. Plant Cell 8, 617–627 (1996). This work reports that SOS1 is essential for salt tolerance in plants.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  4. Shi, H. et al. The Arabidopsis thaliana salt tolerance gene SOS1 encodes a putative Na+/H+ antiporter. Proc. Natl Acad. Sci. USA 97, 6896–6901 (2000). This paper characterizes SOS1 as a Na+/H+ antiporter and its regulation by the SOS2–SOS3 pathway.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  5. Quintero, F. J. et al. Activation of the plasma membrane Na/H antiporter Salt-Overly-Sensitive 1 (SOS1) by phosphorylation of an auto-inhibitory C-terminal domain. Proc. Natl Acad. Sci. USA 108, 2611–2616 (2011). This paper reports the identification of an auto-inhibitory domain in SOS1 and of two key residues regulated by SOS2 kinase.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

Download references

Additional information

Publisher’s note Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations.

This is a summary of: Zhang, X. et al. Structure and activation mechanism of the rice Salt Overly Sensitive 1 (SOS1) Na+/H+ antiporter. Nat. Plants https://doi.org/10.1038/s41477-023-01551-5 (2023).

Rights and permissions

Reprints and permissions

About this article

Check for updates. Verify currency and authenticity via CrossMark

Cite this article

Structural insight into SOS signalling in response to salt stress. Nat. Plants 9, 1793–1794 (2023). https://doi.org/10.1038/s41477-023-01553-3

Download citation

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1038/s41477-023-01553-3

  • Springer Nature Limited

Navigation