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

Result code in 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>
Result on the web
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DOI - Digital Object Identifier
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Result language
angličtina
Original language name
Regulation of plant membrane associated PIP2 - dependent phospholipase D activity by phosphorylation - sborník
Original language description
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
Czech name
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Czech description
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Publication year
2003
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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