Regulation of plant membrane associated PIP2 - dependent phospholipase D activity by phosphorylation - sborník

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22330%2F03%3A00008483" target="_blank" >RIV/60461373:22330/03:00008483 - isvavai.cz</a>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Regulation of plant membrane associated PIP2 - dependent phospholipase D activity by phosphorylation - sborník

Popis výsledku v původním jazyce

Phospholipase D forms the major family of phospholipases that was first discovered and cloned in plants. The distinct biochemical properties of various PLDs might predetermine their different regulation and functions. Several factors have been reported to stimulate plant PLD activity including Ca2+, polyphosphoinositides, G-proteins, N-acylethanolamines, free fatty acids and membrane lipids but nothing is known about the regulatory role of protein modification. In this contribution we would like to present, that covalent modification by phosphorylation could be one of the regulation mechanisms of PLD activity in plants. C2 PIP2-dependent PLD(s) from 5 day hypocotyls of Brassica oleracea var. capitata associated with plasma membrane is probably phosphorylated. Preincubation of plasma membrane fraction with acid phosphatase resulted in concentration´-dependent inhibition of PIP2-dependent PLD activity. Furthermore, we have identified 5 peptide fragments in plasma membrane fraction, which

Název v anglickém jazyce

Regulation of plant membrane associated PIP2 - dependent phospholipase D activity by phosphorylation - sborník

Popis výsledku anglicky

Phospholipase D forms the major family of phospholipases that was first discovered and cloned in plants. The distinct biochemical properties of various PLDs might predetermine their different regulation and functions. Several factors have been reported to stimulate plant PLD activity including Ca2+, polyphosphoinositides, G-proteins, N-acylethanolamines, free fatty acids and membrane lipids but nothing is known about the regulatory role of protein modification. In this contribution we would like to present, that covalent modification by phosphorylation could be one of the regulation mechanisms of PLD activity in plants. C2 PIP2-dependent PLD(s) from 5 day hypocotyls of Brassica oleracea var. capitata associated with plasma membrane is probably phosphorylated. Preincubation of plasma membrane fraction with acid phosphatase resulted in concentration´-dependent inhibition of PIP2-dependent PLD activity. Furthermore, we have identified 5 peptide fragments in plasma membrane fraction, which

Druh

D - Stať ve sborníku

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

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Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2003

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název statě ve sborníku

1 st European Symposium on Plant Lipids

ISBN

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ISSN

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e-ISSN

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Počet stran výsledku

1

Strana od-do

92

Název nakladatele

RWTH Aachen

Místo vydání

Aachen

Místo konání akce

Germany

Datum konání akce

10. 9. 2003

Typ akce podle státní příslušnosti

WRD - Celosvětová akce

Kód UT WoS článku

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