Involvement of phospholipase D and phosphatidic acid in the light-dependent up-regulation of sorghum leaf phosphoenolpyruvate carboxylase-kinase

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...

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Veröffentlicht in:Journal of experimental botany. - 1985. - 61(2010), 10 vom: 25. Juni, Seite 2819-27
1. Verfasser: Monreal, José Antonio (VerfasserIn)
Weitere Verfasser: López-Baena, Francisco Javier, Vidal, Jean, Echevarría, Cristina, García-Mauriño, Sofía
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2010
Zugriff auf das übergeordnete Werk:Journal of experimental botany
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Enzyme Inhibitors Phosphatidic Acids 1-Butanol 8PJ61P6TS3 Protein Kinases EC 2.7.- phosphoenolpyruvate carboxylase kinase EC 2.7.1.- mehr... Protein Serine-Threonine Kinases EC 2.7.11.1 Type C Phospholipases EC 3.1.4.- Phosphoinositide Phospholipase C EC 3.1.4.11 Phospholipase D EC 3.1.4.4 Phosphoenolpyruvate Carboxylase EC 4.1.1.31
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100 1 |a Monreal, José Antonio  |e verfasserin  |4 aut 
245 1 0 |a Involvement of phospholipase D and phosphatidic acid in the light-dependent up-regulation of sorghum leaf phosphoenolpyruvate carboxylase-kinase 
264 1 |c 2010 
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520 |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 
650 4 |a Journal Article 
650 4 |a Research Support, Non-U.S. Gov't 
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650 7 |a Phosphatidic Acids  |2 NLM 
650 7 |a 1-Butanol  |2 NLM 
650 7 |a 8PJ61P6TS3  |2 NLM 
650 7 |a Protein Kinases  |2 NLM 
650 7 |a EC 2.7.-  |2 NLM 
650 7 |a phosphoenolpyruvate carboxylase kinase  |2 NLM 
650 7 |a EC 2.7.1.-  |2 NLM 
650 7 |a Protein Serine-Threonine Kinases  |2 NLM 
650 7 |a EC 2.7.11.1  |2 NLM 
650 7 |a Type C Phospholipases  |2 NLM 
650 7 |a EC 3.1.4.-  |2 NLM 
650 7 |a Phosphoinositide Phospholipase C  |2 NLM 
650 7 |a EC 3.1.4.11  |2 NLM 
650 7 |a Phospholipase D  |2 NLM 
650 7 |a EC 3.1.4.4  |2 NLM 
650 7 |a Phosphoenolpyruvate Carboxylase  |2 NLM 
650 7 |a EC 4.1.1.31  |2 NLM 
700 1 |a López-Baena, Francisco Javier  |e verfasserin  |4 aut 
700 1 |a Vidal, Jean  |e verfasserin  |4 aut 
700 1 |a Echevarría, Cristina  |e verfasserin  |4 aut 
700 1 |a García-Mauriño, Sofía  |e verfasserin  |4 aut 
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773 1 8 |g volume:61  |g year:2010  |g number:10  |g day:25  |g month:06  |g pages:2819-27 
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