"Plant PIP2-dependent phospholipase D activity is regulated by phosphorylation ." . "Hynek, R." . "1"^^ . . "Plant PIP2-dependent phospholipase D activity is regulated by phosphorylation ."@en . "50;54" . . "Plant PIP2-dependent phospholipase D activity is regulated by phosphorylation ." . . "0"^^ . "0"^^ . . . . . "RIV/61389030:_____/03:56033063" . . "554" . . . "Valentov\u00E1, O." . . "1" . "Martinec, Jan" . "Phospholipase D; Phosphorylation; Cytoskeleton"@en . "P(LN00A081), Z(AV0Z5038910), Z(MSM 223300006)" . . "Novotn\u00E1, Z." . "Linek, J." . "Potock\u00FD, M." . "5"^^ . . "Plant PIP2-dependent phospholipase D activity is regulated by phosphorylation ."@en . "621026" . "6"^^ . . "0014-5793" . . "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" . "RIV/61389030:_____/03:56033063!RIV/2004/AV0/A56004/N" . . "NL - Nizozemsko" . "FEBS Letters" . "[D02F60A5E32B]" . . "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 . .