Please use this identifier to cite or link to this item: doi:10.22028/D291-30941
Title: 14-3-3 Proteins and Other Candidates form Protein-Protein Interactions with the Cytosolic C-terminal End of SOS1 Affecting Its Transport Activity
Author(s): Duscha, Kerstin
Martins Rodrigues, Cristina
Müller, Maria
Wartenberg, Ruth
Fliegel, Larry
Deitmer, Joachim W.
Jung, Martin
Zimmermann, Richard
Neuhaus, H. Ekkehard
Language: English
Title: International Journal of Molecular Sciences
Volume: 21
Issue: 9
Publisher/Platform: MDPI
Year of Publication: 2020
Free key words: Arabidopsis
salt tolerance
salt-overly sensitive (SOS1)
14-3-3 proteins
membrane transporter
DDC notations: 610 Medicine and health
Publikation type: Journal Article
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.
DOI of the first publication: 10.3390/ijms21093334
Link to this record: urn:nbn:de:bsz:291--ds-309416
ISSN: 1422-0067
Date of registration: 18-Dec-2020
Description of the related object: Supplementary Materials
Related object:
Faculty: M - Medizinische Fakultät
Department: M - Medizinische Biochemie und Molekularbiologie
Professorship: M - Keiner Professur zugeordnet
Collections:SciDok - Der Wissenschaftsserver der Universität des Saarlandes

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