ArticleThe Plant cell2001
Molecular characterization of functional domains in the protein kinase SOS2 that is required for plant salt tolerance.
Article in The Plant cell, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 221 papers.
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221 citing papers in PubMed, 457 citations in OpenAlex.
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- Calcium signaling-mediated phosphorylation controls zinc allocation in Arabidopsis.Stress biology · 2025Article
- Protein Post-Translational Modifications in Plant Abiotic Stress Responses.Plants (Basel, Switzerland) · 2025Review
- Alfalfa MsSOS2 confers salinity tolerance by promoting lateral root growth and regulating NaScientific reports · 2025Article
- Salt stress activates the CDK8-AHL10-SUVH2/9 module to dynamically regulate salt tolerance in Arabidopsis.Nature communications · 2025Article
- SALT OVERLY SENSITIVE2 and AMMONIUM TRANSPORTER1;1 contribute to plant salt tolerance by maintaining ammonium uptake.The Plant cell · 2025Article
- Salinity survival: molecular mechanisms and adaptive strategies in plants.Frontiers in plant science · 2025Review
- Transcriptome Analysis of the Regulatory Mechanisms of Holly (Plants (Basel, Switzerland) · 2024Article
- The role of CBL-CIPK signaling in plant responses to biotic and abiotic stresses.Plant molecular biology · 2024Review
- Proteomic profiling ofPhysiology and molecular biology of plants : an international journal of functional plant biology · 2024Article
- The proteome landscape of the root cap reveals a role for the jacalin-associated lectin JAL10 in the salt-induced endoplasmic reticulum stress pathway.Plant communications · 2023Article
- Structure and activation mechanism of the rice Salt Overly Sensitive 1 (SOS1) NaNature plants · 2023Article
- Structural basis for the activity regulation of Salt Overly Sensitive 1 in Arabidopsis salt tolerance.Nature plants · 2023Article
- CIPK15-mediated inhibition of NHHeliyon · 2023Article
- Phosphorylation of RhoGDI1, a Rho GDP dissociation inhibitor, regulates root hair development inProceedings of the National Academy of Sciences of the United States of America · 2023Article
- SALT OVERLY SENSITIVE2 stabilizes phytochrome-interacting factors PIF4 and PIF5 to promote Arabidopsis shade avoidance.The Plant cell · 2023Article
- Phytochromes enhance SOS2-mediated PIF1 and PIF3 phosphorylation and degradation to promote Arabidopsis salt tolerance.The Plant cell · 2023Article
- Deciphering the complex cotton genome for improving fiber traits and abiotic stress resilience in sustainable agriculture.Molecular biology reports · 2023Review
161 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The SOS3 (for SALT OVERLY SENSITIVE3) calcium binding protein and SOS2 protein kinase are required for sodium and potassium ion homeostasis and salt tolerance in Arabidopsis. We have shown previously that SOS3 interacts with and activates the SOS2 protein kinase. We report here the identification of a SOS3 binding motif in SOS2 that also serves as the kinase autoinhibitory domain. Yeast two-hybrid assays as well as in vitro binding assays revealed a 21-amino acid motif in the regulatory domain of SOS2 that is necessary and sufficient for interaction with SOS3. Database searches revealed a large family of SOS2-like protein kinases containing such a SOS3 binding motif. Using a yeast two-hybrid system, we show that these SOS2-like kinases interact with members of the SOS3 family of calcium binding proteins. Two-hybrid assays also revealed interaction between the N-terminal kinase domain and the C-terminal regulatory domain within SOS2, suggesting that the regulatory domain may inhibit kinase activity by blocking substrate access to the catalytic site. Removal of the regulatory domain of SOS2, including the SOS3 binding motif, resulted in constitutive activation of the protein kinase, indicating that the SOS3 binding motif can serve as a kinase autoinhibitory domain. Constitutively active SOS2 that is SOS3 independent also was produced by changing Thr(168) to Asp in the activation loop of the SOS2 kinase domain. Combining the Thr(168)-to-Asp mutation with the autoinhibitory domain deletion created a superactive SOS2 kinase. These results provide insights into regulation of the kinase activities of SOS2 and the SOS2 family of protein kinases.
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