Plant PIP2-dependent phospholipase D activity is regulated by phosphorylation

Kód výsledku v 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>

Nalezeny alternativní kódy

RIV/61389030:_____/03:56033063

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Plant PIP2-dependent phospholipase D activity is regulated by phosphorylation

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

Plant PIP2-dependent phospholipase D activity is regulated by phosphorylation

Popis výsledku anglicky

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.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

<a href="/cs/project/LN00A081" target="_blank" >LN00A081: Signální dráhy u rostlin</a><br>

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 periodika

FEBS Letters

ISSN

ISSN 0014-579

e-ISSN

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Svazek periodika

2003

Číslo periodika v rámci svazku

554

Stát vydavatele periodika

BE - Belgické království

Počet stran výsledku

5

Strana od-do

50-54

Kód UT WoS článku

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EID výsledku v databázi Scopus

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