Abstract
The Salt Overly Sensitive (SOS) pathway regulates intracellular sodium ion (Na(+)) homeostasis and salt tolerance in plants. Until recently, little was known about the mechanisms that inhibit the SOS pathway when plants are grown in the absence of salt stress. In this study, we report that the Arabidopsis thaliana 14-3-3 proteins λ and κ interact with SOS2 and repress its kinase activity. Growth in the presence of salt decreases the interaction between SOS2 and the 14-3-3 proteins, leading to kinase activation in planta. 14-3-3 λ interacts with the SOS2 junction domain, which is important for its kinase activity. A phosphorylation site (Ser-294) is identified within this domain by mass spectrometry. Mutation of Ser-294 to Ala or Asp does not affect SOS2 kinase activity in the absence of the 14-3-3 proteins. However, in the presence of 14-3-3 proteins, the inhibition of SOS2 activity is decreased by the Ser-to-Ala mutation and enhanced by the Ser-to-Asp exchange. These results identify 14-3-3 λ and κ as important regulators of salt tolerance. The inhibition of SOS2 mediated by the binding of 14-3-3 proteins represents a novel mechanism that confers basal repression of the SOS pathway in the absence of salt stress.
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Claims 10
Claim · model-written summary
14-3-3 proteins lambda and kappa interact with SOS2 and repress its kinase activity in Arabidopsis.
- Taxon
- Arabidopsis thaliana
Arabidopsis thalianae0 - Gene
- SOS2e0
- Outcome
- kinase activitye0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“the Arabidopsis thaliana 14-3-3 proteins λ and κ interact with SOS2 and repress its kinase activity”
Claim · model-written summary
Growth in the presence of salt decreased the interaction between SOS2 and the 14-3-3 proteins.
- Taxon
- Arabidopsis thalianaArabidopsis thalianae0
- Treatment
- Growth in the presence of salte1
- Gene
- SOS2e1
- Outcome
- the interaction between SOS2 and the 14-3-3 proteinse1
- Direction
- decreasese1
Not reportedComparator
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“the Arabidopsis thaliana 14-3-3 proteins λ and κ interact with SOS2 and repress its kinase activity”
e1“Growth in the presence of salt decreases the interaction between SOS2 and the 14-3-3 proteins, leading to kinase activation in planta”
Claim · model-written summary
Growth in the presence of salt led to SOS2 kinase activation in planta.
- Taxon
- Arabidopsis thalianaArabidopsis thalianae0
- Treatment
- Growth in the presence of salte1
- Gene
- SOS2e1
- Outcome
- kinase activatione1
- Direction
- increaseinferrede1
Not reportedComparator
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“the Arabidopsis thaliana 14-3-3 proteins λ and κ interact with SOS2 and repress its kinase activity”
e1“Growth in the presence of salt decreases the interaction between SOS2 and the 14-3-3 proteins, leading to kinase activation in planta”
Claim · model-written summary
The SOS2 junction domain, which 14-3-3 lambda binds, is important for SOS2 kinase activity.
- Taxon
- Arabidopsis thalianaArabidopsis thalianae0
- Gene
- SOS2 junction domaine2
- Outcome
- kinase activitye2
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“the Arabidopsis thaliana 14-3-3 proteins λ and κ interact with SOS2 and repress its kinase activity”
e2“14-3-3 λ interacts with the SOS2 junction domain, which is important for its kinase activity”
Claim · model-written summary
Ser-294 is identified as a phosphorylation site within the SOS2 junction domain by mass spectrometry.
- Taxon
- Arabidopsis thalianaArabidopsis thalianae0
- Outcome
- phosphorylation site (Ser-294)e3
- Qualifier
- by mass spectrometrye3
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“the Arabidopsis thaliana 14-3-3 proteins λ and κ interact with SOS2 and repress its kinase activity”
e3“A phosphorylation site (Ser-294) is identified within this domain by mass spectrometry”
Claim · model-written summary
Mutation of Ser-294 to Ala or Asp does not affect SOS2 kinase activity in the absence of 14-3-3 proteins.
- Taxon
- Arabidopsis thalianaArabidopsis thalianae0
- Treatment
- Mutation of Ser-294 to Ala or Aspe4
- Gene
- SOS2e4
- Outcome
- SOS2 kinase activitye4
- Direction
- does not affecte4
- Qualifier
- in the absence of the 14-3-3 proteinse4
Not reportedComparator
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“the Arabidopsis thaliana 14-3-3 proteins λ and κ interact with SOS2 and repress its kinase activity”
e4“Mutation of Ser-294 to Ala or Asp does not affect SOS2 kinase activity in the absence of the 14-3-3 proteins”
Claim · model-written summary
The Ser-to-Ala mutation decreased the 14-3-3-mediated inhibition of SOS2 activity.
- Taxon
- Arabidopsis thalianaArabidopsis thalianae0
- Treatment
- Ser-to-Ala mutatione5
- Gene
- SOS2e5
- Outcome
- inhibition of SOS2 activitye5
- Direction
- decreasede5
- Qualifier
- in the presence of 14-3-3 proteinse5
Not reportedComparator
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“the Arabidopsis thaliana 14-3-3 proteins λ and κ interact with SOS2 and repress its kinase activity”
e5“in the presence of 14-3-3 proteins, the inhibition of SOS2 activity is decreased by the Ser-to-Ala mutation and enhanced by the Ser-to-Asp exchange”
Claim · model-written summary
The Ser-to-Asp exchange enhanced the 14-3-3-mediated inhibition of SOS2 activity.
- Taxon
- Arabidopsis thalianaArabidopsis thalianae0
- Treatment
- Ser-to-Asp exchangee5
- Gene
- SOS2e5
- Outcome
- inhibition of SOS2 activitye5
- Direction
- enhancede5
- Qualifier
- in the presence of 14-3-3 proteinse5
Not reportedComparator
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“the Arabidopsis thaliana 14-3-3 proteins λ and κ interact with SOS2 and repress its kinase activity”
e5“in the presence of 14-3-3 proteins, the inhibition of SOS2 activity is decreased by the Ser-to-Ala mutation and enhanced by the Ser-to-Asp exchange”
Claim · model-written summary
14-3-3 lambda and kappa are important regulators of salt tolerance in Arabidopsis.
- Taxon
- Arabidopsis thalianaArabidopsis thalianae0
- Gene
- 14-3-3 λ and κe6
- Outcome
- salt tolerancee6
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“the Arabidopsis thaliana 14-3-3 proteins λ and κ interact with SOS2 and repress its kinase activity”
e6“These results identify 14-3-3 λ and κ as important regulators of salt tolerance”
Claim · model-written summary
Binding of 14-3-3 proteins gives basal repression of the SOS pathway in the absence of salt stress.
- Taxon
- Arabidopsis thalianaArabidopsis thalianae0
- Gene
- 14-3-3 proteinse7
- Outcome
- basal repression of the SOS pathwaye7
- Qualifier
- in the absence of salt stresse7
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“the Arabidopsis thaliana 14-3-3 proteins λ and κ interact with SOS2 and repress its kinase activity”
e7“The inhibition of SOS2 mediated by the binding of 14-3-3 proteins represents a novel mechanism that confers basal repression of the SOS pathway in the absence of salt stress”
The same questions in other papers
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- no effect
- negative
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See all 7 papers →Claims are grouped by organism, treatment and what was measured or targeted. A paper counts as positive when any of its claims in the group is positive.