About: Plant PIP2-dependent phospholipase D activity is regulated by phosphorylation .     Goto   Sponge   NotDistinct   Permalink

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  • Phospholipase D (PLD) 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 phosphatidylinositol-4,5-bisphosphate (PIP2)-dependent PLD(s) from 5 day hypocotyls of Brassica oleracea associated with plasma membrane is covalently modified-phosphorylated. Pre-incubation of the plasma membrane fraction with acid phosphatase resulted in concentration-dependent inhibition of PIP2-dependent PLD activity. Using matrix-assisted laser desorption/ionization time of flight mass spectrometry of tryptic in-gel digests, the BoPLD1,2 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 in the mass of the phosphate group (80 Da) were revealed: TMQMMYQTIYK, EVADGTVSVYNSPR and KASKSRGLGK which possess five potential Ser/Thr phosphorylation sites. Our findings suggest that a phosphorylation/dephosphorylation
  • Phospholipase D (PLD) 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 phosphatidylinositol-4,5-bisphosphate (PIP2)-dependent PLD(s) from 5 day hypocotyls of Brassica oleracea associated with plasma membrane is covalently modified-phosphorylated. Pre-incubation of the plasma membrane fraction with acid phosphatase resulted in concentration-dependent inhibition of PIP2-dependent PLD activity. Using matrix-assisted laser desorption/ionization time of flight mass spectrometry of tryptic in-gel digests, the BoPLD1,2 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 in the mass of the phosphate group (80 Da) were revealed: TMQMMYQTIYK, EVADGTVSVYNSPR and KASKSRGLGK which possess five potential Ser/Thr phosphorylation sites. Our findings suggest that a phosphorylation/dephosphorylation (en)
Title
  • Plant PIP2-dependent phospholipase D activity is regulated by phosphorylation .
  • Plant PIP2-dependent phospholipase D activity is regulated by phosphorylation . (en)
skos:prefLabel
  • Plant PIP2-dependent phospholipase D activity is regulated by phosphorylation .
  • Plant PIP2-dependent phospholipase D activity is regulated by phosphorylation . (en)
skos:notation
  • RIV/61389030:_____/03:56033063!RIV/2004/AV0/A56004/N
http://linked.open.../vavai/riv/strany
  • 50;54
http://linked.open...avai/riv/aktivita
http://linked.open...avai/riv/aktivity
  • P(LN00A081), Z(AV0Z5038910), Z(MSM 223300006)
http://linked.open...iv/cisloPeriodika
  • 1
http://linked.open...vai/riv/dodaniDat
http://linked.open...aciTvurceVysledku
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  • 621026
http://linked.open...ai/riv/idVysledku
  • RIV/61389030:_____/03:56033063
http://linked.open...riv/jazykVysledku
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  • Phospholipase D; Phosphorylation; Cytoskeleton (en)
http://linked.open.../riv/klicoveSlovo
http://linked.open...odStatuVydavatele
  • NL - Nizozemsko
http://linked.open...ontrolniKodProRIV
  • [D02F60A5E32B]
http://linked.open...i/riv/nazevZdroje
  • FEBS Letters
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http://linked.open...vavai/riv/projekt
http://linked.open...UplatneniVysledku
http://linked.open...v/svazekPeriodika
  • 554
http://linked.open...iv/tvurceVysledku
  • Hynek, R.
  • Martinec, Jan
  • Novotná, Z.
  • Valentová, O.
  • Linek, J.
  • Potocký, M.
http://linked.open...n/vavai/riv/zamer
issn
  • 0014-5793
number of pages
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