| pubmed-article:12070350 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12070350 | lifeskim:mentions | umls-concept:C0043393 | lld:lifeskim |
| pubmed-article:12070350 | lifeskim:mentions | umls-concept:C0162741 | lld:lifeskim |
| pubmed-article:12070350 | lifeskim:mentions | umls-concept:C0019868 | lld:lifeskim |
| pubmed-article:12070350 | lifeskim:mentions | umls-concept:C0086982 | lld:lifeskim |
| pubmed-article:12070350 | lifeskim:mentions | umls-concept:C0597484 | lld:lifeskim |
| pubmed-article:12070350 | pubmed:issue | 13 | lld:pubmed |
| pubmed-article:12070350 | pubmed:dateCreated | 2002-6-26 | lld:pubmed |
| pubmed-article:12070350 | 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. | lld:pubmed |
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| pubmed-article:12070350 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12070350 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12070350 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:12070350 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12070350 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:12070350 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:12070350 | pubmed:author | pubmed-author:QuinteroFranc... | lld:pubmed |
| pubmed-article:12070350 | pubmed:author | pubmed-author:PardoJose MJM | lld:pubmed |
| pubmed-article:12070350 | pubmed:author | pubmed-author:ZhuJian-KangJ... | lld:pubmed |
| pubmed-article:12070350 | pubmed:author | pubmed-author:ShiHuazhongH | lld:pubmed |
| pubmed-article:12070350 | pubmed:author | pubmed-author:OhtaMasaruM | lld:pubmed |
| pubmed-article:12070350 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12070350 | pubmed:day | 25 | lld:pubmed |
| pubmed-article:12070350 | pubmed:volume | 99 | lld:pubmed |
| pubmed-article:12070350 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12070350 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12070350 | pubmed:pagination | 9061-6 | lld:pubmed |
| pubmed-article:12070350 | pubmed:dateRevised | 2010-9-14 | lld:pubmed |
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| pubmed-article:12070350 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:12070350 | pubmed:articleTitle | Reconstitution in yeast of the Arabidopsis SOS signaling pathway for Na+ homeostasis. | lld:pubmed |
| pubmed-article:12070350 | pubmed:affiliation | Instituto de Recursos Naturales y Agrobiologia, Consejo Superior de Investigaciones Cientificas, Sevilla 41080, Spain. | lld:pubmed |
| pubmed-article:12070350 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12070350 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:12070350 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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