Abstract
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.
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Claims 8
Claim · model-written summary
Elicitor stimulation rapidly changed protein phosphorylation in tomato cells.
- Taxon
- tomato
Solanum lycopersicume0 - Organ / stage
- cellse0
- Treatment
- elicitor-treatede0
- Outcome
- protein phosphorylatione0
- Direction
- drastic changese0
Not reportedComparator
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“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.”
Claim · model-written summary
K-252a and staurosporine prevented elicitor-induced phosphorylation changes.
- Taxon
- plant cellst0
- Treatment
- K-252a and staurosporinee0
- Outcome
- changes in protein phosphorylatione0
- Direction
- completely preventede0
Not reportedComparator
Verbatim
e0“The protein kinase inhibitors K-252a and staurosporine completely prevented these elicitor-induced changes in protein phosphorylation.”
t0“plant cells”
Claim · model-written summary
K-252a and staurosporine blocked elicitor-induced extracellular alkalinization.
- Taxon
- plant cellst0
- Treatment
- K-252a and staurosporinee0
- Outcome
- extracellular alkalinizatione0
- Direction
- blockede0
Not reportedComparator
Verbatim
e0“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.”
t0“plant cells”
Claim · model-written summary
K-252a and staurosporine blocked elicitor-induced ethylene biosynthesis.
- Taxon
- plant cellst0
- Treatment
- K-252a and staurosporinee0
- Outcome
- biosynthesis of ethylenee0
- Direction
- blockede0
Not reportedComparator
Verbatim
e0“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.”
t0“plant cells”
Claim · model-written summary
Inhibition of elicitor responses correlated with inhibition of tomato microsomal protein kinase.
- Taxon
- tomatoSolanum lycopersicume0
- Treatment
- K-252a, staurosporine, and benzoylated staurosporine derivativese0
- Gene
- tomato microsomal protein kinasee0
- Outcome
- elicitor responses in vivoe0
Not reportedDirection
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“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.”
Claim · model-written summary
K-252a added after labeling caused newly labeled phosphoprotein radioactivity to disappear within minutes.
- Taxon
- plant cellst0
- Treatment
- K-252ae0
- Outcome
- radioactivity in certain newly labeled phosphoprotein bandse0
- Direction
- disappearede0
- Qualifier
- 1 min after the[32] phosphatee0
Not reportedComparator
Verbatim
e0“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.”
t0“plant cells”
Claim · model-written summary
K-252a applied during elicitation arrested alkalinization within minutes.
- Taxon
- plant cellst0
- Treatment
- K-252ae0
- Outcome
- alkalinizatione0
- Direction
- arreste0
- Qualifier
- in midcourse of elicitatione0
Not reportedComparator
Verbatim
e0“This correlated with an arrest of alkalinization within minutes when K-252a was applied in midcourse of elicitation.”
t0“plant cells”
Claim · model-written summary
K-252a-sensitive kinase phosphorylation is asserted to be essential for elicitor signal transduction and maintenance.
Verbatim
e0“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.”
The same questions in other papers
staurosporine · molecular: expression · Solanum lycopersicum (tomato)Results agree
1 paper in the same direction as this paper
- no effect
K-252a · molecular: expression · Solanum lycopersicum (tomato)Results agree
2 papers in the same direction as this paper
- negative
- negative
Claims are grouped by organism, treatment and what was measured or targeted. A paper counts as positive when any of its claims in the group is positive.