| pubmed-article:11607219 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11607219 | lifeskim:mentions | umls-concept:C0032098 | lld:lifeskim |
| pubmed-article:11607219 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
| pubmed-article:11607219 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
| pubmed-article:11607219 | lifeskim:mentions | umls-concept:C1710082 | lld:lifeskim |
| pubmed-article:11607219 | lifeskim:mentions | umls-concept:C1160185 | lld:lifeskim |
| pubmed-article:11607219 | lifeskim:mentions | umls-concept:C0392747 | lld:lifeskim |
| pubmed-article:11607219 | lifeskim:mentions | umls-concept:C1314939 | lld:lifeskim |
| pubmed-article:11607219 | lifeskim:mentions | umls-concept:C0439831 | lld:lifeskim |
| pubmed-article:11607219 | pubmed:issue | 19 | lld:pubmed |
| pubmed-article:11607219 | pubmed:dateCreated | 2001-10-18 | lld:pubmed |
| pubmed-article:11607219 | pubmed:abstractText | Plant cells have an acute sense for pathogen-derived chemical stimuli, so-called elicitors, which induce the plant's defense response. To investigate the molecular basis of chemosensory transduction, elicitor-treated tomato cells were labeled with 1-min pulses of [32P] phosphate. This technique revealed drastic changes in protein phosphorylation in vivo within minutes of stimulation. The protein kinase inhibitors K-252a and staurosporine completely prevented these elicitor-induced changes in protein phosphorylation. They also blocked two early biochemical responses to elicitors, extracellular alkalinization and biosynthesis of ethylene. The ability of K-252a, staurosporine, and benzoylated staurosporine derivatives to inhibit elicitor responses in vivo correlated with their ability to inhibit tomato microsomal protein kinase in vitro. When K-252a was given to elicited cells 1 min after the[32] phosphate, the radioactivity in certain newly labeled phosphoprotein bands disappeared again within minutes. This correlated with an arrest of alkalinization within minutes when K-252a was applied in midcourse of elicitation. These data show that phosphorylation of protein substrates by K-252a-sensitive protein kinases is essential for transduction of elicitor signals in plant cells and that continuous phosphorylation of these proteins is required to maintain the elicited state. | lld:pubmed |
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| pubmed-article:11607219 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11607219 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11607219 | pubmed:status | PubMed-not-MEDLINE | lld:pubmed |
| pubmed-article:11607219 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:11607219 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:11607219 | pubmed:author | pubmed-author:FeligPP | lld:pubmed |
| pubmed-article:11607219 | pubmed:author | pubmed-author:BolleaGG | lld:pubmed |
| pubmed-article:11607219 | pubmed:author | pubmed-author:RegenassMM | lld:pubmed |
| pubmed-article:11607219 | pubmed:author | pubmed-author:GrosskopfD... | lld:pubmed |
| pubmed-article:11607219 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11607219 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:11607219 | pubmed:volume | 88 | lld:pubmed |
| pubmed-article:11607219 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11607219 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11607219 | pubmed:pagination | 8831-4 | lld:pubmed |
| pubmed-article:11607219 | pubmed:dateRevised | 2010-9-14 | lld:pubmed |
| pubmed-article:11607219 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:11607219 | pubmed:articleTitle | Rapid changes of protein phosphorylation are involved in transduction of the elicitor signal in plant cells. | lld:pubmed |
| pubmed-article:11607219 | pubmed:affiliation | Friedrich Miescher-Institut, Basel, Switzerland. | lld:pubmed |
| pubmed-article:11607219 | pubmed:publicationType | Journal Article | lld:pubmed |
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