Plant PIP2-dependent phospholipase D activity is regulated by phosphorylation

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22330%2F03%3A00008482" target="_blank" >RIV/60461373:22330/03:00008482 - isvavai.cz</a>
Alternative codes found
RIV/61389030:_____/03:56033063
Result on the web
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DOI - Digital Object Identifier
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Result language
angličtina
Original language name
Plant PIP2-dependent phospholipase D activity is regulated by phosphorylation
Original language description
Phospholipase D forms the major family of phospholipases that was first discovered and cloned in plants. In this report we have shown for the first time, that C2 PIP2-dependent PLD(s) from 5 days hypocotyls of Brassica oleracea associated with plasma membrane is covalently modified-phosphorylated. Pre-incubation of plasma membrane fraction with acid phosphatase resulted in concentration-dependent inhibition of PIP2-dependent PLD activity. Using MALDI-TOF mass spectrometry of tryptic in-gel digests, BoPLD?1,2 isoform was identified. Comparing the spectra of the proteins obtained from the plasma membrane fractions treated and non-treated with acid phosphatase, three peptides differing by mass of phosphate group (80 Da) were revealed: TMQMMYQTIYK, EVADGTVSVYNSPR and KASKSRGLGK which posses five potential Ser/Thr phosphorylation sites. Our findings suggest that phosphorylation/dephosphorylation mechanism may be involved in regulation of plant PIP2-dependent PLD activity.
Czech name
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Czech description
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Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
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Project
<a href="/en/project/LN00A081" target="_blank" >LN00A081: Signaling pathways in plants</a><br>
Continuities
Z - Vyzkumny zamer (s odkazem do CEZ)

Publication year
2003
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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