Source:http://linkedlifedata.com/resource/pubmed/id/11607219
Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
19
|
| pubmed:dateCreated |
2001-10-18
|
| 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.
|
| pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/11607219-11537471,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11607219-16578842,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11607219-16593852,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11607219-2163028,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11607219-2261987,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11607219-2318857,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11607219-2530218,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11607219-2541432,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11607219-2554892,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11607219-2556636,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11607219-2672462,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11607219-2714889,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11607219-3113737,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11607219-5432063
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:status |
PubMed-not-MEDLINE
|
| pubmed:month |
Oct
|
| pubmed:issn |
0027-8424
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
1
|
| pubmed:volume |
88
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
8831-4
|
| pubmed:dateRevised |
2010-9-14
|
| pubmed:year |
1991
|
| pubmed:articleTitle |
Rapid changes of protein phosphorylation are involved in transduction of the elicitor signal in plant cells.
|
| pubmed:affiliation |
Friedrich Miescher-Institut, Basel, Switzerland.
|
| pubmed:publicationType |
Journal Article
|