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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
13
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pubmed:dateCreated |
2002-6-26
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pubmed:abstractText |
The Arabidopsis thaliana SOS1 protein is a putative Na+/H+ antiporter that functions in Na+ extrusion and is essential for the NaCl tolerance of plants. sos1 mutant plants share phenotypic similarities with mutants lacking the protein kinase SOS2 and the Ca2+ sensor SOS3. To investigate whether the three SOS proteins function in the same response pathway, we have reconstituted the SOS system in yeast cells. Expression of SOS1 improved the Na+ tolerance of yeast mutants lacking endogenous Na+ transporters. Coexpression of SOS2 and SOS3 dramatically increased SOS1-dependent Na+ tolerance, whereas SOS2 or SOS3 individually had no effect. The SOS2/SOS3 kinase complex promoted the phosphorylation of SOS1. A constitutively active form of SOS2 phosphorylated SOS1 in vitro independently of SOS3, but could not fully substitute for the SOS2/SOS3 kinase complex for activation of SOS1 in vivo. Further, we show that SOS3 recruits SOS2 to the plasma membrane. Although sos1 mutant plants display defective K+ uptake at low external concentrations, neither the unmodified nor the SOS2/SOS3-activated SOS1 protein showed K+ transport capacity in vivo, suggesting that the role of SOS1 on K+ uptake is indirect. Our results provide an example of functional reconstitution of a plant response pathway in a heterologous system and demonstrate that the SOS1 ion transporter, the SOS2 protein kinase, and its associated Ca2+ sensor SOS3 constitute a functional module. We propose a model in which SOS3 activates and directs SOS2 to the plasma membrane for the stimulatory phosphorylation of the Na+ transporter SOS1.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/12070350-10692635,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12070350-10725350,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12070350-10725382,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12070350-10748251,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12070350-10767428,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12070350-10823923,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12070350-11006339,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12070350-11080272,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12070350-11402167,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12070350-11597497,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12070350-11884687,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12070350-1767589,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12070350-1833392,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12070350-2906717,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12070350-6310322,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12070350-6384187,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12070350-7656990,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12070350-7905477,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12070350-8154181,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12070350-9154808,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12070350-9234672,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12070350-9296500,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12070350-9614085,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12070350-9632394,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12070350-9802016
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
99
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
9061-6
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pubmed:dateRevised |
2010-9-14
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pubmed:meshHeading |
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pubmed:year |
2002
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pubmed:articleTitle |
Reconstitution in yeast of the Arabidopsis SOS signaling pathway for Na+ homeostasis.
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pubmed:affiliation |
Instituto de Recursos Naturales y Agrobiologia, Consejo Superior de Investigaciones Cientificas, Sevilla 41080, Spain.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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