We report the high-resolution cryo-electron microscopy structures of SOS1, a major determinant of salt tolerance in plants. From our structural and functional analyses, we propose a model for how the unique large cytoplasmic domain regulates the Na+/H+ exchange activity of SOS1, enhancing our understanding of the mechanisms underpinning the regulation of SOS1 activity.
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References
Yang, Y. & Guo, Y. Unraveling salt stress signaling in plants. J. Integr. Plant Biol. 60, 796–804 (2018). A review article that presents the plant salt tolerance and SOS1 pathway.
Wu, S. J., Ding, L. & Zhu, J. K. SOS1, a genetic locus essential for salt tolerance and potassium acquisition. Plant Cell 8, 617–627 (1996). This paper determined SOS1 for the first time.
Shi, H., Ishitani, M., Kim, C. & Zhu, J.-K. The Arabidopsis thaliana salt tolerance gene SOS1 encodes a putative Na+/H+ antiporter. Proc. Natl Acad. Sci. USA 97, 6896–6901 (2000). This paper reports SOS1 as a Na+/H+ exchanger and describes sos1 mutations.
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 that SOS1 is activated through phosphorylation by SOS2 and also identifies the SOS2 phosphorylation sites.
Cha, J.-Y. et al. The Na+/H+ antiporter SALT OVERLY SENSITIVE 1 regulates salt compensation of circadian rhythms by stabilizing GIGANTEA in Arabidopsis. Proc. Natl Acad. Sci. USA 119 (2022). This paper reports the interaction of SOS1 with GIGANTEA.
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This is a summary of: Zhang, Y. et al. Structural basis for the activity regulation of Salt Overly Sensitive 1 in Arabidopsis salt tolerance. Nat. Plants https://doi.org/10.1038/s41477-023-01550-6 (2023).
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Structural and functional insight into the regulation of SOS1 activity. Nat. Plants 9, 1791–1792 (2023). https://doi.org/10.1038/s41477-023-01552-4
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DOI: https://doi.org/10.1038/s41477-023-01552-4
