The hydrophobic segment of <i>Arabidopsis thaliana</i> cluster I diacylglycerol kinases is sufficient to target the proteins to cell membranes

Vaultier, Marie‐Noëlle; Cantrel, Catherine; Guerbette, F.; Boutté, Yohann; Vergnolle, Chantal; Çiçek, Dominique; Bolte, Susanne; Zachowski, Alain; Ruelland, Éric

doi:10.1016/j.febslet.2008.04.042

Cited by 25 publications

(28 citation statements)

References 22 publications

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“…OsDGK(4, 5, 8) and AtDGK(1, 2) belong to cluster I, which possesses two cysteine-rich domains conferring C1 domains. These domains are absent from other Arabidopsis and rice DGKs (Figure 2; Vaultier et al, 2008). The C1 domain can bind to proteins to modulate the interaction with lipids and proteins (Colon-Gonzalez and Kazanietz, 2006).…”

Section: Discussionmentioning

confidence: 99%

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The Rice Diacylglycerol Kinase Family: Functional Analysis Using Transient RNA Interference

Ge¹,

Chen²,

Jing³

et al. 2012

Front. Plant Sci.

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Diacylglycerol kinase (DGK) is a pivotal enzyme that phosphorylates diacylglycerol (DAG) to form phosphatidic acid (PA). The production of PA from phospholipase D (PLD) and the coupled phospholipase C/DGK route is an important signaling process in animal and plant cells. In this study, we report a genomic analysis of eight putative rice DGKs encoded by a gene family (OsDGKs) grouped into three clusters. To further investigate the functions of the OsDGKs, a double-stranded RNA (dsRNA)-induced RNA silencing method was established. Introduction of in vitro-synthesized dsRNAs corresponding to a unique or conserved region of OsDGKs into rice protoplasts abolished or diminished the expression of individual or multiple OsDGK genes. Suppressing the expression of OsDGKs resulted in a distinct depletion of the transcripts of the defense gene OsNPR1 and the salt-responsive gene OsCIPK15. Our primary results suggest that OsDGKs are involved in the signaling of stress responses.

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Section: Discussionmentioning

confidence: 99%

“…In Arabidopsis , AtDGK2 and AtDGK7 have been biochemically characterized (Gómez-Merino et al, 2004, 2005). A hydrophobic segment at the N-termini of AtDGK1 and AtDGK2 is necessary to target the resulting proteins to endoplasmic reticulum (ER) membranes (Vaultier et al, 2008). …”

Section: Introductionmentioning

confidence: 99%

The Rice Diacylglycerol Kinase Family: Functional Analysis Using Transient RNA Interference

Ge¹,

Chen²,

Jing³

et al. 2012

Front. Plant Sci.

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“…This molecule was shown to inhibit in vitro DGK either from plants (Lundberg and Sommarin, 1992; Gómez-Merino et al, 2005; Vaultier et al, 2008) or from animals (Lundberg and Sommarin, 1992; Matowe and Ginsberg, 1996; Jiang et al, 2000; Gómez-Merino et al, 2005). The in vivo synthesis of cold-induced PA was reduced by treatment with R59022 in Arabidopsis suspension cells (Ruelland et al, 2002); R59022 enhanced phytoalexin accumulation in pea ( Pisum sativum ) treated with fungal elicitor (Toyoda et al, 2000).…”

Section: Discussionmentioning

confidence: 99%

The Arabidopsis DREB2 genetic pathway is constitutively repressed by basal phosphoinositide-dependent phospholipase C coupled to diacylglycerol kinase

Djafi¹,

Vergnolle²,

Cantrel³

et al. 2013

Front. Plant Sci.

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Phosphoinositide-dependent phospholipases C (PI-PLCs) are activated in response to various stimuli. They utilize substrates provided by type III-Phosphatidylinositol-4 kinases (PI4KIII) to produce inositol triphosphate and diacylglycerol (DAG) that is phosphorylated into phosphatidic acid (PA) by DAG-kinases (DGKs). The roles of PI4KIIIs, PI-PLCs, and DGKs in basal signaling are poorly understood. We investigated the control of gene expression by basal PI-PLC pathway in Arabidopsis thaliana suspension cells. A transcriptome-wide analysis allowed the identification of genes whose expression was altered by edelfosine, 30 μM wortmannin, or R59022, inhibitors of PI-PLCs, PI4KIIIs, and DGKs, respectively. We found that a gene responsive to one of these molecules is more likely to be similarly regulated by the other two inhibitors. The common action of these agents is to inhibit PA formation, showing that basal PI-PLCs act, in part, on gene expression through their coupling to DGKs. Amongst the genes up-regulated in presence of the inhibitors, were some DREB2 genes, in suspension cells and in seedlings. The DREB2 genes encode transcription factors with major roles in responses to environmental stresses, including dehydration. They bind to C-repeat motifs, known as Drought-Responsive Elements that are indeed enriched in the promoters of genes up-regulated by PI-PLC pathway inhibitors. PA can also be produced by phospholipases D (PLDs). We show that the DREB2 genes that are up-regulated by PI-PLC inhibitors are positively or negatively regulated, or indifferent, to PLD basal activity. Our data show that the DREB2 genetic pathway is constitutively repressed in resting conditions and that DGK coupled to PI-PLC is active in this process, in suspension cells and seedlings. We discuss how this basal negative regulation of DREB2 genes is compatible with their stress-triggered positive regulation.

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“…From this homogenate, nuclei were isolated as in [45] and [46]. Chloroplasts were isolated according to [47].…”

Section: Methodsmentioning

confidence: 99%

“…Mitochondria were obtained according to [48]. From microsomes, we isolated either plasma membranes, or detergent-resistant membranes, or endoplasmic reticulum and Golgi membranes or tonoplasts [31], [46], [49]–[51]. A schematic representation of the cell fractionation procedure leading to the different membranes is given in Figure S8.…”

Section: Methodsmentioning

confidence: 99%

Acyl Chains of Phospholipase D Transphosphatidylation Products in Arabidopsis Cells: A Study Using Multiple Reaction Monitoring Mass Spectrometry

et al. 2012

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BackgroundPhospholipases D (PLD) are major components of signalling pathways in plant responses to some stresses and hormones. The product of PLD activity is phosphatidic acid (PA). PAs with different acyl chains do not have the same protein targets, so to understand the signalling role of PLD it is essential to analyze the composition of its PA products in the presence and absence of an elicitor.Methodology/Principal findingsPotential PLD substrates and products were studied in Arabidopsis thaliana suspension cells treated with or without the hormone salicylic acid (SA). As PA can be produced by enzymes other than PLD, we analyzed phosphatidylbutanol (PBut), which is specifically produced by PLD in the presence of n-butanol. The acyl chain compositions of PBut and the major glycerophospholipids were determined by multiple reaction monitoring (MRM) mass spectrometry. PBut profiles of untreated cells or cells treated with SA show an over-representation of 160/18∶2- and 16∶0/18∶3-species compared to those of phosphatidylcholine and phosphatidylethanolamine either from bulk lipid extracts or from purified membrane fractions. When microsomal PLDs were used in in vitro assays, the resulting PBut profile matched exactly that of the substrate provided. Therefore there is a mismatch between the acyl chain compositions of putative substrates and the in vivo products of PLDs that is unlikely to reflect any selectivity of PLDs for the acyl chains of substrates.ConclusionsMRM mass spectrometry is a reliable technique to analyze PLD products. Our results suggest that PLD action in response to SA is not due to the production of a stress-specific molecular species, but that the level of PLD products per se is important. The over-representation of 160/18∶2- and 16∶0/18∶3-species in PLD products when compared to putative substrates might be related to a regulatory role of the heterogeneous distribution of glycerophospholipids in membrane sub-domains.

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The hydrophobic segment of Arabidopsis thaliana cluster I diacylglycerol kinases is sufficient to target the proteins to cell membranes

Cited by 25 publications

References 22 publications

The Rice Diacylglycerol Kinase Family: Functional Analysis Using Transient RNA Interference

The Rice Diacylglycerol Kinase Family: Functional Analysis Using Transient RNA Interference

The Arabidopsis DREB2 genetic pathway is constitutively repressed by basal phosphoinositide-dependent phospholipase C coupled to diacylglycerol kinase

Acyl Chains of Phospholipase D Transphosphatidylation Products in Arabidopsis Cells: A Study Using Multiple Reaction Monitoring Mass Spectrometry

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