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PMID: 10725350 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

The Arabidopsis SOS2 protein kinase physically interacts with and is activated by the calcium-binding protein SOS3.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 97 ·No. 7 ·2000-03-28 ·Pages 3735-40

Halfter U, Ishitani M, Zhu JK

Abstract

The Arabidopsis thaliana SOS2 and SOS3 genes are required for intracellular Na(+) and K(+) homeostasis and plant tolerance to high Na(+) and low K(+) environments. SOS3 is an EF hand type calcium-binding protein having sequence similarities with animal neuronal calcium sensors and the yeast calcineurin B. SOS2 is a serine/threonine protein kinase in the SNF1/AMPK family. We report here that SOS3 physically interacts with and activates SOS2 protein kinase. Genetically, sos2sos3 double mutant analysis indicates that SOS2 and SOS3 function in the same pathway. Biochemically, SOS2 interacts with SOS3 in the yeast two-hybrid system and in vitro binding assays. The interaction is mediated by the C-terminal regulatory domain of SOS2. SOS3 activates SOS2 protein kinase activity in a Ca(2+)-dependent manner. Therefore, SOS3 and SOS2 define a novel regulatory pathway important for the control of intracellular ion homeostasis and salt tolerance in plants.

MeSH Terms
Amino Acid Sequence Arabidopsis/enzymology Arabidopsis Proteins Base Sequence Calcium/metabolism DNA Primers Enzyme Activation Molecular Sequence Data Plant Proteins/metabolism Protein Binding Protein Serine-Threonine Kinases/chemistry,genetics,metabolism Sequence Homology, Amino Acid Two-Hybrid System Techniques
Chemicals
Arabidopsis Proteins DNA Primers Plant Proteins SOS3 protein, Arabidopsis SOS2 protein, Arabidopsis Protein Serine-Threonine Kinases Calcium
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Halfter U
Department of Plant Sciences, University of Arizona, Tucson, AZ 85721, USA.
Ishitani M
Zhu J K
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.040577697
Published
2000-03-28
Pages
3735-40
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC16309
Subset
IM
Grants
NIGMS NIH HHS · R01 GM059138 · United States
NIGMS NIH HHS · R01GM59138 · United States
External Links
PubMed source DOI: 10.1073/pnas.040577697 PMC Full Text View journal details
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