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14-3-3 Proteins and Other Candidates form Protein-Protein Interactions with the Cytosolic C-terminal End of SOS1 Affecting Its Transport Activity

The plasma membrane transporter SOS1 (SALT-OVERLY SENSITIVE1) is vital for plant survival under salt stress. SOS1 activity is tightly regulated, but little is known about the underlying mechanism. SOS1 contains a cytosolic, autoinhibitory C-terminal tail (abbreviated as SOS1 C-term), which is target...

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Autores principales: Duscha, Kerstin, Martins Rodrigues, Cristina, Müller, Maria, Wartenberg, Ruth, Fliegel, Larry, Deitmer, Joachim W., Jung, Martin, Zimmermann, Richard, Neuhaus, H. Ekkehard
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7246916/
https://www.ncbi.nlm.nih.gov/pubmed/32397251
http://dx.doi.org/10.3390/ijms21093334
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author Duscha, Kerstin
Martins Rodrigues, Cristina
Müller, Maria
Wartenberg, Ruth
Fliegel, Larry
Deitmer, Joachim W.
Jung, Martin
Zimmermann, Richard
Neuhaus, H. Ekkehard
author_facet Duscha, Kerstin
Martins Rodrigues, Cristina
Müller, Maria
Wartenberg, Ruth
Fliegel, Larry
Deitmer, Joachim W.
Jung, Martin
Zimmermann, Richard
Neuhaus, H. Ekkehard
author_sort Duscha, Kerstin
collection PubMed
description The plasma membrane transporter SOS1 (SALT-OVERLY SENSITIVE1) is vital for plant survival under salt stress. SOS1 activity is tightly regulated, but little is known about the underlying mechanism. SOS1 contains a cytosolic, autoinhibitory C-terminal tail (abbreviated as SOS1 C-term), which is targeted by the protein kinase SOS2 to trigger its transport activity. Here, to identify additional binding proteins that regulate SOS1 activity, we synthesized the SOS1 C-term domain and used it as bait to probe Arabidopsis thaliana cell extracts. Several 14-3-3 proteins, which function in plant salt tolerance, specifically bound to and interacted with the SOS1 C-term. Compared to wild-type plants, when exposed to salt stress, Arabidopsis plants overexpressing SOS1 C-term showed improved salt tolerance, significantly reduced Na(+) accumulation in leaves, reduced induction of the salt-responsive gene WRKY25, decreased soluble sugar, starch, and proline levels, less impaired inflorescence formation and increased biomass. It appears that overexpressing SOS1 C-term leads to the sequestration of inhibitory 14-3-3 proteins, allowing SOS1 to be more readily activated and leading to increased salt tolerance. We propose that the SOS1 C-term binds to previously unknown proteins such as 14-3-3 isoforms, thereby regulating salt tolerance. This finding uncovers another regulatory layer of the plant salt tolerance program.
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spelling pubmed-72469162020-06-02 14-3-3 Proteins and Other Candidates form Protein-Protein Interactions with the Cytosolic C-terminal End of SOS1 Affecting Its Transport Activity Duscha, Kerstin Martins Rodrigues, Cristina Müller, Maria Wartenberg, Ruth Fliegel, Larry Deitmer, Joachim W. Jung, Martin Zimmermann, Richard Neuhaus, H. Ekkehard Int J Mol Sci Article The plasma membrane transporter SOS1 (SALT-OVERLY SENSITIVE1) is vital for plant survival under salt stress. SOS1 activity is tightly regulated, but little is known about the underlying mechanism. SOS1 contains a cytosolic, autoinhibitory C-terminal tail (abbreviated as SOS1 C-term), which is targeted by the protein kinase SOS2 to trigger its transport activity. Here, to identify additional binding proteins that regulate SOS1 activity, we synthesized the SOS1 C-term domain and used it as bait to probe Arabidopsis thaliana cell extracts. Several 14-3-3 proteins, which function in plant salt tolerance, specifically bound to and interacted with the SOS1 C-term. Compared to wild-type plants, when exposed to salt stress, Arabidopsis plants overexpressing SOS1 C-term showed improved salt tolerance, significantly reduced Na(+) accumulation in leaves, reduced induction of the salt-responsive gene WRKY25, decreased soluble sugar, starch, and proline levels, less impaired inflorescence formation and increased biomass. It appears that overexpressing SOS1 C-term leads to the sequestration of inhibitory 14-3-3 proteins, allowing SOS1 to be more readily activated and leading to increased salt tolerance. We propose that the SOS1 C-term binds to previously unknown proteins such as 14-3-3 isoforms, thereby regulating salt tolerance. This finding uncovers another regulatory layer of the plant salt tolerance program. MDPI 2020-05-08 /pmc/articles/PMC7246916/ /pubmed/32397251 http://dx.doi.org/10.3390/ijms21093334 Text en © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Duscha, Kerstin
Martins Rodrigues, Cristina
Müller, Maria
Wartenberg, Ruth
Fliegel, Larry
Deitmer, Joachim W.
Jung, Martin
Zimmermann, Richard
Neuhaus, H. Ekkehard
14-3-3 Proteins and Other Candidates form Protein-Protein Interactions with the Cytosolic C-terminal End of SOS1 Affecting Its Transport Activity
title 14-3-3 Proteins and Other Candidates form Protein-Protein Interactions with the Cytosolic C-terminal End of SOS1 Affecting Its Transport Activity
title_full 14-3-3 Proteins and Other Candidates form Protein-Protein Interactions with the Cytosolic C-terminal End of SOS1 Affecting Its Transport Activity
title_fullStr 14-3-3 Proteins and Other Candidates form Protein-Protein Interactions with the Cytosolic C-terminal End of SOS1 Affecting Its Transport Activity
title_full_unstemmed 14-3-3 Proteins and Other Candidates form Protein-Protein Interactions with the Cytosolic C-terminal End of SOS1 Affecting Its Transport Activity
title_short 14-3-3 Proteins and Other Candidates form Protein-Protein Interactions with the Cytosolic C-terminal End of SOS1 Affecting Its Transport Activity
title_sort 14-3-3 proteins and other candidates form protein-protein interactions with the cytosolic c-terminal end of sos1 affecting its transport activity
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7246916/
https://www.ncbi.nlm.nih.gov/pubmed/32397251
http://dx.doi.org/10.3390/ijms21093334
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