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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.
Duscha, Kerstin; Martins Rodrigues, Cristina; Müller, Maria; Wartenberg, Ruth; Fliegel, Larry; Deitmer, Joachim W; Jung, Martin; Zimmermann, Richard; Neuhaus, H Ekkehard.
Afiliação
  • Duscha K; Department of Plant Physiology, University of Kaiserslautern, Erwin-Schrödinger-Str., D-67653 Kaiserslautern, Germany.
  • Martins Rodrigues C; Department of Plant Physiology, University of Kaiserslautern, Erwin-Schrödinger-Str., D-67653 Kaiserslautern, Germany.
  • Müller M; Department of Plant Physiology, University of Kaiserslautern, Erwin-Schrödinger-Str., D-67653 Kaiserslautern, Germany.
  • Wartenberg R; Department of Plant Physiology, University of Kaiserslautern, Erwin-Schrödinger-Str., D-67653 Kaiserslautern, Germany.
  • Fliegel L; Department of Biochemistry, Faculty of Medicine & Dentistry, University of Alberta, 347 Medical Sciences Building, Edmonton, AB T6G 2H7, Canada.
  • Deitmer JW; Department of Zoology, University of Kaiserslautern, Erwin-Schrödinger-Str., D-67653 Kaiserslautern, Germany.
  • Jung M; Department of Medical Biochemistry and Molecular Biology, Medical Faculty, Saarland University, D-66421 Homburg, Germany.
  • Zimmermann R; Department of Medical Biochemistry and Molecular Biology, Medical Faculty, Saarland University, D-66421 Homburg, Germany.
  • Neuhaus HE; Department of Plant Physiology, University of Kaiserslautern, Erwin-Schrödinger-Str., D-67653 Kaiserslautern, Germany.
Int J Mol Sci ; 21(9)2020 May 08.
Article em En | MEDLINE | ID: mdl-32397251
ABSTRACT
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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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Membrana Celular / Arabidopsis / Trocadores de Sódio-Hidrogênio / Proteínas de Arabidopsis / Proteínas 14-3-3 / Tolerância ao Sal Idioma: En Ano de publicação: 2020 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Membrana Celular / Arabidopsis / Trocadores de Sódio-Hidrogênio / Proteínas de Arabidopsis / Proteínas 14-3-3 / Tolerância ao Sal Idioma: En Ano de publicação: 2020 Tipo de documento: Article