pubmed-article:19716822 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:19716822 | lifeskim:mentions | umls-concept:C0162741 | lld:lifeskim |
pubmed-article:19716822 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
pubmed-article:19716822 | lifeskim:mentions | umls-concept:C0033640 | lld:lifeskim |
pubmed-article:19716822 | lifeskim:mentions | umls-concept:C0068355 | lld:lifeskim |
pubmed-article:19716822 | lifeskim:mentions | umls-concept:C1419697 | lld:lifeskim |
pubmed-article:19716822 | pubmed:issue | 18 | lld:pubmed |
pubmed-article:19716822 | pubmed:dateCreated | 2009-9-15 | lld:pubmed |
pubmed-article:19716822 | pubmed:abstractText | The plant hormone abscisic acid (ABA) triggers production of reactive oxygen species (ROS) in guard cells via the AtrbohD and AtrbohF NADPH oxidases, leading to stomatal closure. The ABA-activated SnRK2 protein kinase open stomata 1 (OST1) (SRK2E/SnRK2.6) acts upstream of ROS in guard cell ABA signaling. Here, we report that OST1 phosphorylates Ser13 and Ser174 on AtrbohF. In addition, substitution of Ser174 to Ala results in a approximately 40% reduction in the phosphorylation of AtrbohF by OST1. We also show that OST1 physically interacts with AtrbohF. These results provide biochemical evidence suggesting that OST1 regulates AtrbohF activity. | lld:pubmed |
pubmed-article:19716822 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19716822 | pubmed:language | eng | lld:pubmed |
pubmed-article:19716822 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19716822 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:19716822 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19716822 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19716822 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19716822 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19716822 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19716822 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19716822 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19716822 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:19716822 | pubmed:month | Sep | lld:pubmed |
pubmed-article:19716822 | pubmed:issn | 1873-3468 | lld:pubmed |
pubmed-article:19716822 | pubmed:author | pubmed-author:AroAA | lld:pubmed |
pubmed-article:19716822 | pubmed:author | pubmed-author:MerlotSylvain... | lld:pubmed |
pubmed-article:19716822 | pubmed:author | pubmed-author:KwakJune MJM | lld:pubmed |
pubmed-article:19716822 | pubmed:author | pubmed-author:ZivyMichelM | lld:pubmed |
pubmed-article:19716822 | pubmed:author | pubmed-author:HuHeng-ChengH... | lld:pubmed |
pubmed-article:19716822 | pubmed:author | pubmed-author:DavantureMarl... | lld:pubmed |
pubmed-article:19716822 | pubmed:author | pubmed-author:ValotBenoîtB | lld:pubmed |
pubmed-article:19716822 | pubmed:author | pubmed-author:LeungJeffreyJ | lld:pubmed |
pubmed-article:19716822 | pubmed:author | pubmed-author:SirichandraCa... | lld:pubmed |
pubmed-article:19716822 | pubmed:author | pubmed-author:LeeSangmeeS | lld:pubmed |
pubmed-article:19716822 | pubmed:author | pubmed-author:DjaouiMichaël... | lld:pubmed |
pubmed-article:19716822 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:19716822 | pubmed:day | 17 | lld:pubmed |
pubmed-article:19716822 | pubmed:volume | 583 | lld:pubmed |
pubmed-article:19716822 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:19716822 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:19716822 | pubmed:pagination | 2982-6 | lld:pubmed |
pubmed-article:19716822 | pubmed:dateRevised | 2009-12-3 | lld:pubmed |
pubmed-article:19716822 | pubmed:meshHeading | pubmed-meshheading:19716822... | lld:pubmed |
pubmed-article:19716822 | pubmed:meshHeading | pubmed-meshheading:19716822... | lld:pubmed |
pubmed-article:19716822 | pubmed:meshHeading | pubmed-meshheading:19716822... | lld:pubmed |
pubmed-article:19716822 | pubmed:meshHeading | pubmed-meshheading:19716822... | lld:pubmed |
pubmed-article:19716822 | pubmed:meshHeading | pubmed-meshheading:19716822... | lld:pubmed |
pubmed-article:19716822 | pubmed:meshHeading | pubmed-meshheading:19716822... | lld:pubmed |
pubmed-article:19716822 | pubmed:meshHeading | pubmed-meshheading:19716822... | lld:pubmed |
pubmed-article:19716822 | pubmed:meshHeading | pubmed-meshheading:19716822... | lld:pubmed |
pubmed-article:19716822 | pubmed:year | 2009 | lld:pubmed |
pubmed-article:19716822 | pubmed:articleTitle | Phosphorylation of the Arabidopsis AtrbohF NADPH oxidase by OST1 protein kinase. | lld:pubmed |
pubmed-article:19716822 | pubmed:affiliation | Institut des Sciences du Végétal, Centre National de la Recherche Scientifique, UPR 2355, Gif-sur-Yvette, France. | lld:pubmed |
pubmed-article:19716822 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:19716822 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
pubmed-article:19716822 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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