Ca2+ ions and lysophospholipids activate phosphorylation of different proteins in plasma membranes and tonoplast

Scherer, Günther F. E.; Hecker, Doris; Müller, Lost

doi:10.1016/s0176-1617(11)81247-2

Cited by 13 publications

(12 citation statements)

References 46 publications

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“…LPC is known to activate the H ϩ -transporting ATPase of the plasma membrane (Palmgren and Sommarin, 1989), probably by stimulating the staurosporine-sensitive phosphorylation of this enzyme (Scherer et al, 1993;Hanju et al, 1996;Xing et al, 1996). In contrast, the rapid interaction of LPC with the vacuolar Na ϩ and H ϩ transport seen in our experiments was not changed by staurosporine (which, however, may not exclude any phosphorylation of involved proteins).…”

Section: Discussioncontrasting

confidence: 49%

Elicitor-Activated Phospholipase A₂ Generates Lysophosphatidylcholines That Mobilize the Vacuolar H⁺ Pool for pH Signaling via the Activation of Na⁺-Dependent Proton Fluxes

2002

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Section: Discussioncontrasting

confidence: 49%

Elicitor-Activated Phospholipase A₂ Generates Lysophosphatidylcholines That Mobilize the Vacuolar H⁺ Pool for pH Signaling via the Activation of Na⁺-Dependent Proton Fluxes

2002

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“…It is possible that at least one of the mechanisms of PLA action is through the regulatory effects of its hydrolytic products, lysophospholipids, and fatty acids on H ϩ transport and ion permeability of the plasma membrane (Palmgren et al, 1988;Palmgren and Sommarin, 1989;Scherer et al, 1993;Chyb et al, 1999). Membrane depolarization and ion fluxes are among the earliest events observed in tomato cells after wounding or elicitor treatments (Thain et al, 1990;Felix et al, 1993;Felix and Boller, 1995;Moyen and Johannes, 1996;Schaller and Oecking, 1999).…”

Section: Discussionmentioning

confidence: 99%

“…The hydrolytic products of PLA activity, lysophospholipids, and free fatty acids also have been shown to modulate the activity of several membrane-associated enzymes, including NADH oxidase (Brightman et al, 1991), 1,3-␤ -D -glucan synthase (Kauss and Jeblick, 1986), protein kinases (Martiny-Baron and Scherer, 1989;Scherer et al, 1993), ion channels (Chyb et al, 1999), and ATPases (Palmgren et al, 1988;Palmgren and Sommarin, 1989;Scherer et al, 1993). Several of these enzymes have been implicated in different plant defense reactions, including the regulation of H ϩ -ATPase activity during plant-pathogen interactions, elicitor treatments, and wounding (Vera-Estrella et al, 1994;Xing et al, 1996;Schaller and Oecking, 1999).…”

Section: Introductionmentioning

confidence: 99%

Positional Specificity of a Phospholipase A Activity Induced by Wounding, Systemin, and Oligosaccharide Elicitors in Tomato Leaves

1999

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Phospholipase A (PLA) activity, as measured by the accumulation of 14 C-lysophosphatidylcholine in leaves of tomato plants, increased rapidly and systemically in response to wounding. The increase in PLA activity in the systemic unwounded leaves was biphasic in wild-type tomato plants, peaking at 15 min and again at 60 min, but the second peak of activity was absent in transgenic prosystemin antisense plants. Supplying young excised tomato plants with the polypeptide hormone systemin also caused 14 C-lysophosphatidylcholine to increase to levels similar to those induced by wounding, but the increase in activity persisted for Ͼ 2 hr. Antagonists of systemin blocked both the release of 14 Clysophosphatidylcholine and the accumulation of defense proteins in response to systemin. 14 C-lysophosphatidylcholine levels did not increase in response to jasmonic acid. Chemical acylation of the lysophosphatidylcholine produced by wounding, systemin, and oligosaccharide elicitors followed by enzymatic hydrolysis with lipases of known specificities demostrated that the lysophosphatidylcholine is generated by a PLA with specificity for the sn-2 position.

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“…6. In addition, the internalisation of plasma membrane vesicles may account for the presence of the second immuno-reactive band in the seed coat protoplast extracts which may correspond to a degradation product of the H +-ATPase (Palmgren et al 1990, Scherer et al 1993). In the Vicia seed coat, the strongest mRNA locatisation and immunolabelling for SBP was confined to the thin-walled parenchyma transfer cells .…”

Section: Discussionmentioning

confidence: 99%

“…This band may correspond to a putative degradation product (Pahngren et at. 1990, Scherer et at. 1993.…”

Section: Sds-page and Western-blot Analysesmentioning

confidence: 99%

Cell specific expression of three genes involved in plasma membrane sucrose transport in developingVicia faba seed

et al. 1997

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Summary. In developing seeds of Viciafaba, transfer ceils line the inner surface of the seed coat and the juxtaposed epidermal surface of the cotyledons. Circumstantial evidence, derived from anatomical and physiological studies, indicates that these cells are the likely sites of sucrose efflux to, and influx from, the seed apoplasm, respectively. In this study, expression of an H+/sucrose symporter-gene was found to be localised to the epidermal-transfer cell complexes of the cotyledons. The sucrose binding protein (SBP) gene was expressed in these ceils as well as in the thin-walled parenchyma transfer cells of the seed coat. SBP was immunolocalised exclusively to the plasma membranes located in the wall ingrowth regions of the transfer cells. In addition, a plasma membrane H+-ATPase was most abundant in the wall ingrowth regions with decreasing levels of expression at increasing distance from the transfer cell layers. The observed co-localisation of high densities of a plasma membrane tt+-ATPase and sucrose transport proteins to the wall ingrowths of the seed coat and cotyledon transfer cells provides strong evidence that these regions are the principal sites of facilitated membrane transport of sucrose to and from the seed apoplasm.Keywords: Gene expression; Plasma membrane transport; Seed; Sucrose efflux/influx; Transfer ceils; Vicia faba.Abbreviations: BCIP 5-bromo-4-chloro-3-indolyl phosphate; DIG digoxigenin; H+-ATPase plasma membrane H+-translocating adenosine triphosphatase; Ig immunoglobulin; LeSUTt tomato H+/sucrose symporter; SBP sucrose binding protein.

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Ca2+ ions and lysophospholipids activate phosphorylation of different proteins in plasma membranes and tonoplast

Cited by 13 publications

References 46 publications

Elicitor-Activated Phospholipase A₂ Generates Lysophosphatidylcholines That Mobilize the Vacuolar H⁺ Pool for pH Signaling via the Activation of Na⁺-Dependent Proton Fluxes

Elicitor-Activated Phospholipase A₂ Generates Lysophosphatidylcholines That Mobilize the Vacuolar H⁺ Pool for pH Signaling via the Activation of Na⁺-Dependent Proton Fluxes

Positional Specificity of a Phospholipase A Activity Induced by Wounding, Systemin, and Oligosaccharide Elicitors in Tomato Leaves

Cell specific expression of three genes involved in plasma membrane sucrose transport in developingVicia faba seed

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Ca2+ ions and lysophospholipids activate phosphorylation of different proteins in plasma membranes and tonoplast

Cited by 13 publications

References 46 publications

Elicitor-Activated Phospholipase A2 Generates Lysophosphatidylcholines That Mobilize the Vacuolar H+ Pool for pH Signaling via the Activation of Na+-Dependent Proton Fluxes

Elicitor-Activated Phospholipase A2 Generates Lysophosphatidylcholines That Mobilize the Vacuolar H+ Pool for pH Signaling via the Activation of Na+-Dependent Proton Fluxes

Positional Specificity of a Phospholipase A Activity Induced by Wounding, Systemin, and Oligosaccharide Elicitors in Tomato Leaves

Cell specific expression of three genes involved in plasma membrane sucrose transport in developingVicia faba seed

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Elicitor-Activated Phospholipase A₂ Generates Lysophosphatidylcholines That Mobilize the Vacuolar H⁺ Pool for pH Signaling via the Activation of Na⁺-Dependent Proton Fluxes

Elicitor-Activated Phospholipase A₂ Generates Lysophosphatidylcholines That Mobilize the Vacuolar H⁺ Pool for pH Signaling via the Activation of Na⁺-Dependent Proton Fluxes