0172355 - UEB-Q 20033063 RIV NL eng J - Článek v odborném periodiku
Novotná, Z. - Linek, J. - Hynek, R. - Martinec, Jan - Potocký, M. - Valentová, O.
Plant PIP2-dependent phospholipase D activity is regulated by phosphorylation.
FEBS Letters. Roč. 554, č. 1 (2003), s. 50-54. ISSN 0014-5793. E-ISSN 1873-3468
Grant CEP: GA MŠMT LN00A081
Výzkumný záměr: CEZ:AV0Z5038910
Klíčová slova: Phospholipase D * Phosphorylation * Cytoskeleton
Kód oboru RIV: CE - Biochemie
Impakt faktor: 3.609, rok: 2003

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 mechanism may be involved in the regulation of plant PIP2-dependent PLD activity.
Trvalý link: http://hdl.handle.net/11104/0069394