Signal Transduction in Leaf Movement

Coté, Gary G.

doi:10.1104/pp.109.3.729

Cited by 88 publications

(58 citation statements)

References 20 publications

(32 reference statements)

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“…Early research on osmo-stress-induced lipid signalling implicated phospholipase C (PLC) activation. The potential signals generated ± inositol 1,4,5-trisphosphate (InsP 3 ), diacyl glycerol (DAG) and Ca 2+ ± are thought to cause cell shrinkage (reviewed by Cote Â , 1995;Munnik et al, 1998a). Whether DAG is directly involved in signalling is dubious, because a protein kinase C (PKC) has not been isolated from plants (Munnik et al, 1998a).…”

Section: Introductionmentioning

confidence: 99%

Hyperosmotic stress stimulates phospholipase D activity and elevates the levels of phosphatidic acid and diacylglycerol pyrophosphate

et al. 2000

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SummaryIn mammalian cells, phospholipase D (PLD) and its product phosphatidic acid (PA) are involved in a number of signalling cascades, including cell proliferation, membrane traf®cking and defence responses. In plant cells a signalling role for PLD and PA is also emerging. Plants have the extra ability to phosphorylate PA to produce diacylglycerol pyrophosphate (DGPP), a newly discovered phospholipid whose formation attenuates PA levels, but which could itself be a second messenger. Here we report that increases in PA and its conversion to DGPP are common stress responses to water de®cit. Increases occur within minutes of treatment and are dependent on the level of stress. Part of the PA produced is due to PLD activity as measured by the in vivo transphosphatidylation of 1-butanol, and part is due to diacylglycerol kinase activity as monitored via 32 P-PA formation in a differential labelling protocol. Increases in PA and DGPP are found not only in the green alga Chlamydomonas moewusii and cellsuspension cultures of tomato and alfalfa when subjected to hyperosmotic stress, but also in dehydrated leaves of the resurrection plant Craterostigma plantagineum. These results provide further evidence that PLD and PA play a role in plant signalling, and provide the ®rst demonstration that DGPP is formed during physiological conditions that evoke PA synthesis.

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Section: Introductionmentioning

confidence: 99%

Hyperosmotic stress stimulates phospholipase D activity and elevates the levels of phosphatidic acid and diacylglycerol pyrophosphate

et al. 2000

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“…These channels show high selectivity for K 1 over other monovalent cations, and are reputed to specifically mediate K 1 uptake and transport in plant cells (Gambale and Uozumi, 2006). K 1 channels and transport systems play multiple roles in higher-plant processes, including opening and closing of stomatal pores, leaf movements, and ion uptake in roots (Hedrich and Becker, 1994;Schroeder et al, 1994;Coté, 1995). AKT1 is an inward-rectifying channel for K 1 uptake in Arabidopsis roots.…”

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confidence: 99%

Rice Shaker Potassium Channel OsKAT1 Confers Tolerance to Salinity Stress on Yeast and Rice Cells

Obata

Kitamoto²,

Nakamura³

et al. 2007

Plant Physiol.

145

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We screened a rice (Oryza sativa L. 'Nipponbare') full-length cDNA expression library through functional complementation in yeast (Saccharomyces cerevisiae) to find novel cation transporters involved in salt tolerance. We found that expression of a cDNA clone, encoding the rice homolog of Shaker family K 1 channel KAT1 (OsKAT1), suppressed the salt-sensitive phenotype of yeast strain G19 (Dena1-4), which lacks a major component of Na 1 efflux. It also suppressed a K 1 -transport-defective phenotype of yeast strain CY162 (Dtrk1Dtrk2), suggesting the enhancement of K 1 uptake by OsKAT1. By the expression of OsKAT1, the K 1 contents of salt-stressed G19 cells increased during the exponential growth phase. At the linear phase, however, OsKAT1-expressing G19 cells accumulated less Na 1 than nonexpressing cells, but almost the same K 1 . The cellular Na 1 to K 1 ratio of OsKAT1-expressing G19 cells remained lower than nonexpressing cells under saline conditions. Rice cells overexpressing OsKAT1 also showed enhanced salt tolerance and increased cellular K 1 content. These functions of OsKAT1 are likely to be common among Shaker K 1 channels because OsAKT1 and Arabidopsis (Arabidopsis thaliana) KAT1 were able to complement the salt-sensitive phenotype of G19 as well as OsKAT1. The expression of OsKAT1 was restricted to internodes and rachides of wild-type rice, whereas other Shaker family genes were expressed in various organs. These results suggest that OsKAT1 is involved in salt tolerance of rice in cooperation with other K 1 channels by participating in maintenance of cytosolic cation homeostasis during salt stress and thus protects cells from Na 1 .

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“…DEAE-cellulose (DE-52), 3MM paper and P-81 paper were purchased from Whatman Ltd. Tween-20, Tween-40, formaldehyde, AgNO 3 and Na 2 CO 3 were purchased from Aldrich. Low molecular mass standards for electrophoresis, Coomassie Brilliant Blue R250 and SDS were supplied by Bio-Rad.…”

Section: Methodsmentioning

confidence: 99%

“…The phosphatidylinositol pathway involves stimulation of a phospholipase C and release of two messengers: diacylglycerol and inositol(1,4,5)-trisphosphate. Diacylglycerol and inositol(1,4,5)trisphosphate are widespread in plant cells, and the levels of diacylglycerol and inositol(1,4,5)trisphosphate are changed during leaf movement [3], when the plants are exposed to the light [4] or during osmotic stress [5,6]. In the animal kingdom the activity of protein kinase C (PKC) is dependent on calcium and phospholipids.…”

mentioning

confidence: 99%

Calcium‐dependent protein kinase from maize seedlings activated by phospholipids

Szczegielniak

Liwosz

Jurkowski

et al. 2000

European Journal of Biochemistry

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A calcium-and phospholipid-dependent protein kinase of apparent molecular mass 54 kDa (designated ZmCPKp54) was partially purified from etiolated maize seedlings. Activity of ZmCPKp54 is stimulated by phosphatidylserine and phosphatidylinositol, but is not essentially affected by diolein and phorbol esters. The enzyme cross-reacts with polyclonal antibodies against the calmodulin like-domain of the calcium-dependent protein kinase, but not with antibodies against catalytic or regulatory domains of protein kinase C. ZmCPKp54 is not able to phosphorylate the specific substrates of protein kinase C (MARCKS peptide and protein kinase C substrate peptide derived from pseudosubstrate sequence) and its activity is not inhibited by specific PKC inhibitors (bisindolylmaleimide, protein kinase C pseudosubstrate inhibitory peptide). The substrate specificity and sensitivity to the inhibitors of the maize enzyme resembles calcium-dependent protein kinase. The biochemical and immunological properties indicate that ZmCPKp54 belongs to the calcium-dependent protein kinase family.Keywords: plant protein kinase; protein kinase specificity; calcium, phosphatidylserine; phosphatidylinositol. In addition, the rapid turnover of phosphatidylinositol (PtdIns) metabolites has been demonstrated in a variety of plant signal responses (reviewed in [2]). The phosphatidylinositol pathway involves stimulation of a phospholipase C and release of two messengers: diacylglycerol and inositol(1,4,5)-trisphosphate. Diacylglycerol and inositol(1,4,5)trisphosphate are widespread in plant cells, and the levels of diacylglycerol and inositol(1,4,5)trisphosphate are changed during leaf movement [3], when the plants are exposed to the light [4] or during osmotic stress [5,6]. In the animal kingdom the activity of protein kinase C (PKC) is dependent on calcium and phospholipids. It is involved in sensing the cellular changes of diacylglycerol and calcium ion concentrations, transducing the signal from the cell membrane to the other signalling components, and finally to the cell nucleus (reviewed in [7]).The presence of elements required for inositol phospholipidbased signalling in plant cells has prompted investigators to look for a calcium-and phospholipid-dependent protein kinase resembling mammalian PKC. The presence of a Ca 12 -and lipid-dependent kinase activity in plants was first shown in cytosolic fraction of zucchini (courgettes) [8] Recently, a 70-kDa protein kinase possessing activity that is stimulated by diacylglycerol or phorbol esters in the presence of calcium was purified to homogenity from etiolated maize leaves [16]. Moreover, a functional homolog of mammalian PKC was identified in potato as a key element in the elicitorinduced defence [18]. The above biochemical and immunological data suggest the existence of PKC counterpart in plants.A large family of calcium-dependent protein kinases (CDPKs), also called calmodulin-like domain protein kinases, is present in plants. These enzymes control many physiological responses and are involved ...

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Signal Transduction in Leaf Movement

Cited by 88 publications

References 20 publications

Hyperosmotic stress stimulates phospholipase D activity and elevates the levels of phosphatidic acid and diacylglycerol pyrophosphate

Hyperosmotic stress stimulates phospholipase D activity and elevates the levels of phosphatidic acid and diacylglycerol pyrophosphate

Rice Shaker Potassium Channel OsKAT1 Confers Tolerance to Salinity Stress on Yeast and Rice Cells

Calcium‐dependent protein kinase from maize seedlings activated by phospholipids

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