A gene encoding a phosphatidylinositol-specific phospholipase C is induced by dehydration and salt stress in Arabidopsis thaliana.

Hirayama, Takashi; Ohto, Chikara; Mizoguchi, Tsuyoshi; Shinozaki, Kazuo

doi:10.1073/pnas.92.9.3903

Cited by 348 publications

(250 citation statements)

References 34 publications

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“…Now most phosphoinositide molecules presented in mammalian cells have been identified in plant cells, and plant genes encoding the PI metabolism enzymes have been cloned in succession, including those for PI synthase [16], PI 3-kinases [17,18], PI4K [19], PIPK [20], PI-PLCs [21,22], inositol polyphosphate phosphatases [23,24], inositol polyphosphate kinases [25,26], and others. In 1998, a cDNA of plant PIPK (AtPIP5K1) from Arabidopsis was cloned, which was the first report of plant PIPK [20].…”

Section: Introductionmentioning

confidence: 99%

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MORN motifs in plant PIPKs are involved in the regulation of subcellular localization and phospholipid binding

Lin

et al. 2006

Cell Res

101

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Multiple repeats of membrane occupation and recognition nexus (MORN) motifs were detected in plant phosphatidylinositl monophosphate kinase (PIPK), a key enzyme in PI-signaling pathway. Structural analysis indicates that all the MORN motifs (with varied numbers at ranges of 7-9), which shared high homologies to those of animal ones, were located at N-terminus and sequentially arranged, except those of OsPIPK1 and AtPIPK7, in which the last MORN motif was separated others by an ~100 amino-acid "island" region, revealing the presence of two kinds of MORN arrangements in plant PIPKs. Through employing a yeast-based SMET (sequence of membrane-targeting) system, the MORN motifs were shown being able to target the fusion proteins to cell plasma membrane, which were further confirmed by expression of fused MORN-GFP proteins. Further detailed analysis via deletion studies indicated the MORN motifs in OsPIPK1, together with the 104 amino-acid "island" region are involved in the regulation of differential subcellular localization, i.e. plasma membrane or nucleus, of the fused proteins. Fat Western blot analysis of the recombinant MORN polypeptide, expressed in Escherichia coli, showed that MORN motifs could strongly bind to PA and relatively slightly to PI4P and PI(4,5)P 2 . These results provide informative hints on mechanisms of subcellular localization, as well as regulation of substrate binding, of plant PIPKs.

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Section: Introductionmentioning

confidence: 99%

“…Several enzymes such as PI synthase and PLC have been demonstrated to be membrane proteins [16,22]. However, some others, including PIPKs, could not be confirmed to be membrane locating based on the physical characteristics of the peptides, although there are some clues that the enzymes are functioned near the cell membranes.…”

Section: Introductionmentioning

confidence: 99%

MORN motifs in plant PIPKs are involved in the regulation of subcellular localization and phospholipid binding

Lin

et al. 2006

Cell Res

101

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“…These ¢ndings suggest that a link might exist between the activation of the plant phosphoinositide system [6] and the elevation of cytosolic Ca 2 . Although it has been known for some time that induction of genes encoding enzymes of the plant phosphoinositide cycle can be triggered by hyperosmotic stress [7,8] little detailed information is currently available about the immediate e¡ects of salt stress and hyperosmotic stress on phosphoinositide-metabolising enzymes and inositol (1,4,5)trisphosphate (Ins(1,4,5)P 3 ) generation. We now describe the e¡ect of salt and osmotic stress on Ins(1,4,5)P 3 production in suspension-cultured carrot (Daucus carota L.) cells.…”

Section: Introductionmentioning

confidence: 99%

Inositol(1,4,5)trisphosphate production in plant cells: an early response to salinity and hyperosmotic stress

Drøbak

Watkins

2000

FEBS Letters

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Salinity and hyperosmotic stress are environmental factors that severely affect the growth and development of plants. Adaptation to these stresses is known to be a complex multistep process, but a rise in cytoplasmic Ca 2+ and increased polyphosphoinositide turnover have now been identified as being amongst the early events leading to the development of tolerance. To determine whether a causal link exists between these two events we have investigated the effects of several salts and osmotic agents on levels of inositol(1,4,5)trisphosphate (Ins(1,4,5)P 3 ) in plant cells. Our data show that salts as well as osmotic agents induce a rapid and up to 15-fold increase in cellular Ins(1,4,5)P 3 levels. The increase in Ins(1,4,5)P 3 occurs in a dose-dependent manner and levels remain elevated for at least 10 min. These data indicate that increased Ins(1,4,5)P 3 production is a common response to salt and hyperosmotic stresses in plants and that it may play an important role in the processes leading to stress tolerance. ß

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“…In Arabidopsis, osmotic stress leads to enhanced expression of AtPLC1 encoding a PtdIns-specific phospholipase C (Hirayama et al, 1995). Moreover, application of salt has been shown to trigger a rapid accumulation of PtdIns(4,5)P 2 and inositol-1,4,5-trisphosphate (De Wald et al, 2001).…”

Section: Involvement Of Phosphoinositide Signaling In Baba-induced Prmentioning

confidence: 99%

Dissecting the β-Aminobutyric Acid–Induced Priming Phenomenon in Arabidopsis

et al. 2005

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Plants treated with the nonprotein amino acid β-aminobutyric acid (BABA) develop an enhanced capacity to resist biotic and abiotic stresses. This BABA-induced resistance (BABA-IR) is associated with an augmented capacity to express basal defense responses, a phenomenon known as priming. Based on the observation that high amounts of BABA induce sterility in Arabidopsis thaliana, a mutagenesis screen was performed to select mutants impaired in BABA-induced sterility (ibs). Here, we report the isolation and subsequent characterization of three T-DNA–tagged ibs mutants. Mutant ibs1 is affected in a cyclin-dependent kinase–like protein, and ibs2 is defective in AtSAC1b encoding a polyphosphoinositide phosphatase. Mutant ibs3 is affected in the regulation of the ABA1 gene encoding the abscisic acid (ABA) biosynthetic enzyme zeaxanthin epoxidase. To elucidate the function of the three IBS genes in plant resistance, the mutants were tested for BABA-IR against the bacterium Pseudomonas syringae pv tomato, the oomycete Hyaloperonospora parasitica, and BABA-induced tolerance to salt. All three ibs mutants were compromised in BABA-IR against H. parasitica, although to a different extent. Whereas ibs1 was reduced in priming for salicylate (SA)-dependent trailing necrosis, mutants ibs2 and ibs3 were affected in the priming for callose deposition. Only ibs1 failed to express BABA-IR against P. syringae, which coincided with a defect in priming for SA-inducible PR-1 gene expression. By contrast, ibs2 and ibs3 showed reduced BABA-induced tolerance to salt, which correlated with an affected priming for ABA-inducible gene expression. For all three ibs alleles, the defects in BABA-induced sterility and BABA-induced protection against P. syringae, H. parasitica, and salt could be confirmed in independent mutants. The data presented here introduce three novel regulatory genes involved in priming for different defense responses.

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A gene encoding a phosphatidylinositol-specific phospholipase C is induced by dehydration and salt stress in Arabidopsis thaliana.

Cited by 348 publications

References 34 publications

MORN motifs in plant PIPKs are involved in the regulation of subcellular localization and phospholipid binding

MORN motifs in plant PIPKs are involved in the regulation of subcellular localization and phospholipid binding

Inositol(1,4,5)trisphosphate production in plant cells: an early response to salinity and hyperosmotic stress

Dissecting the β-Aminobutyric Acid–Induced Priming Phenomenon in Arabidopsis

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