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231223s2010 xx |||||o 00| ||eng c |
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|a 10.1093/jxb/erq114
|2 doi
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|a pubmed24n0658.xml
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|a (DE-627)NLM197522165
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|a (NLM)20410319
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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|a Monreal, José Antonio
|e verfasserin
|4 aut
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|a Involvement of phospholipase D and phosphatidic acid in the light-dependent up-regulation of sorghum leaf phosphoenolpyruvate carboxylase-kinase
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|c 2010
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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|a ƒa Online-Ressource
|b cr
|2 rdacarrier
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|a Date Completed 02.09.2010
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|a Date Revised 03.12.2021
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a The photosynthetic phosphoenolpyruvate carboxylase (C(4)-PEPC) is regulated by phosphorylation by a phosphoenolpyruvate carboxylase kinase (PEPC-k). In Digitaria sanguinalis mesophyll protoplasts, this light-mediated transduction cascade principally requires a phosphoinositide-specific phospholipase C (PI-PLC) and a Ca(2+)-dependent step. The present study investigates the cascade components at the higher integrated level of Sorghum bicolor leaf discs and leaves. PEPC-k up-regulation required light and photosynthetic electron transport. However, the PI-PLC inhibitor U-73122 and inhibitors of calcium release from intracellular stores only partially blocked this process. Analysis of [(32)P]phosphate-labelled phospholipids showed a light-dependent increase in phospholipase D (PLD) activity. Treatment of leaf discs with n-butanol, which decreases the formation of phosphatidic acid (PA) by PLD, led to the partial inhibition of the C(4)-PEPC phosphorylation, suggesting the participation of PLD/PA in the signalling cascade. PPCK1 gene expression was strictly light-dependent. Addition of neomycin or n-butanol decreased, and a combination of both inhibitors markedly reduced PPCK1 expression and the concomitant rise in PEPC-k activity. The calcium/calmodulin antagonist W7 blocked the light-dependent up-regulation of PEPC-k, pointing to a Ca(2+)-dependent protein kinase (CDPK) integrating both second messengers, calcium and PA, which were shown to increase the activity of sorghum CDPK
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Enzyme Inhibitors
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|a Phosphatidic Acids
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|a 1-Butanol
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|a 8PJ61P6TS3
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|a Protein Kinases
|2 NLM
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|a EC 2.7.-
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|a phosphoenolpyruvate carboxylase kinase
|2 NLM
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|a EC 2.7.1.-
|2 NLM
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|a Protein Serine-Threonine Kinases
|2 NLM
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|a EC 2.7.11.1
|2 NLM
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|a Type C Phospholipases
|2 NLM
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|a EC 3.1.4.-
|2 NLM
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|a Phosphoinositide Phospholipase C
|2 NLM
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|a EC 3.1.4.11
|2 NLM
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|a Phospholipase D
|2 NLM
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|a EC 3.1.4.4
|2 NLM
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|a Phosphoenolpyruvate Carboxylase
|2 NLM
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|a EC 4.1.1.31
|2 NLM
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|a López-Baena, Francisco Javier
|e verfasserin
|4 aut
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|a Vidal, Jean
|e verfasserin
|4 aut
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|a Echevarría, Cristina
|e verfasserin
|4 aut
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|a García-Mauriño, Sofía
|e verfasserin
|4 aut
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|i Enthalten in
|t Journal of experimental botany
|d 1985
|g 61(2010), 10 vom: 25. Juni, Seite 2819-27
|w (DE-627)NLM098182706
|x 1460-2431
|7 nnns
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|g volume:61
|g year:2010
|g number:10
|g day:25
|g month:06
|g pages:2819-27
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|u http://dx.doi.org/10.1093/jxb/erq114
|3 Volltext
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|a AR
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|d 61
|j 2010
|e 10
|b 25
|c 06
|h 2819-27
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