ArticleThe Plant cell2000
SOS3 function in plant salt tolerance requires N-myristoylation and calcium binding.
Article in The Plant cell, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 203 papers.
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Who cites it
203 citing papers in PubMed, 523 citations in OpenAlex.
- Overexpression of LotusPlants (Basel, Switzerland) · 2026Article
- Insights into Salinity Stress-Induced Morpho-Physiological and Molecular Responses and Nanoparticle- and Nanobiochar-Mediated Tolerance Mechanisms During Seed Germination.Nanomaterials (Basel, Switzerland) · 2026Review
- N-myristoylation-mediated shuttling of TaMP from plasma membrane to chloroplasts increases wheat susceptibility to rust fungi.Nature plants · 2026Article
- Analysis of salt resistance conferred by salt overly sensitive 3 protein from mulberry (Frontiers in plant science · 2026Article
- Comparative metabolomic and transcriptomic analysis revealing the role of salicylic acid for short-term response with arginine and myristic acid for long-term tolerance under salt stress in watermelon (Frontiers in plant science · 2026Article
- Functional 14-3-3 Proteins: Master Regulators in Plant Responses to Salt Stress.Plants (Basel, Switzerland) · 2025Review
- SOS3 fromCells · 2025Article
- Article
- Genome-wide identification, characterization, and functional analysis of the CHX, SOS, and RLK genes in Solanum lycopersicum under salt stress.Scientific reports · 2025Article
- Salinity survival: molecular mechanisms and adaptive strategies in plants.Frontiers in plant science · 2025Review
- iTRAQ-based proteomic profiling of salt-tolerant and salt-sensitive potato (Frontiers in plant science · 2025Article
- Structural and molecular dynamics simulation studies of CBL-interacting protein kinase CIPK and its complexes related to plant salinity stress.Journal of molecular modeling · 2024Article
- The transcription factor MdERF023 negatively regulates salt tolerance by modulating ABA signaling and NaPlant cell reports · 2024Article
- Molecular cloning and characterization of a salt overly sensitive3 (SOS3) gene from the halophyte Pongamia.Plant molecular biology · 2024Article
- Genome-Wide Identification of Members of the SoybeanPlants (Basel, Switzerland) · 2024Article
- The Roles of Calcineurin B-like Proteins in Plants under Salt Stress.International journal of molecular sciences · 2023Review
- Structure and activation mechanism of the rice Salt Overly Sensitive 1 (SOS1) NaNature plants · 2023Article
- The CALCINEURIN B-LIKE 4/CBL-INTERACTING PROTEIN 3 module degrades repressor JAZ5 during rose petal senescence.Plant physiology · 2023Article
- SALT OVERLY SENSITIVE2 stabilizes phytochrome-interacting factors PIF4 and PIF5 to promote Arabidopsis shade avoidance.The Plant cell · 2023Article
- How Plants Tolerate Salt Stress.Current issues in molecular biology · 2023Review
143 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The salt tolerance gene SOS3 (for salt overly sensitive3) of Arabidopsis is predicted to encode a calcium binding protein with an N-myristoylation signature sequence. Here, we examine the myristoylation and calcium binding properties of SOS3 and their functional significance in plant tolerance to salt. Treatment of young Arabidopsis seedlings with the myristoylation inhibitor 2-hydroxymyristic acid caused the swelling of root tips, mimicking the phenotype of the salt-hypersensitive mutant sos3-1. In vitro translation assays with reticulocyte showed that the SOS3 protein was myristoylated. Targeted mutagenesis of the N-terminal glycine-2 to alanine prevented the myristoylation of SOS3. The functional significance of SOS3 myristoylation was examined by expressing the wild-type myristoylated SOS3 and the mutated nonmyristoylated SOS3 in the sos3-1 mutant. Expression of the myristoylated but not the nonmyristoylated SOS3 complemented the salt-hypersensitive phenotype of sos3-1 plants. No significant difference in membrane association was observed between the myristoylated and nonmyristoylated SOS3. Gel mobility shift and (45)Ca(2)+ overlay assays demonstrated that SOS3 is a unique calcium binding protein and that the sos3-1 mutation substantially reduced the capacity of SOS3 to bind calcium. The resulting mutant SOS3 protein was not able to interact with the SOS2 protein kinase and was less capable of activating it. Together, these results strongly suggest that both N-myristoylation and calcium binding are required for SOS3 function in plant salt tolerance.
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