Plant PIP2‐dependent phospholipase D activity is regulated by phosphorylation

FEBS Letters

Potocký, Martin¹  Hynek, Radovan¹  Martinec, Jan²  Linek, Jan¹  Novotná, Zuzana¹  Valentová, Olga¹ 

[1] Department of Biochemistry and Microbiology, Institute of Chemical Technology Prague, Prague 6, Czech Republic;Institute of Experimental Botany, Academy of Sciences of the Czech Republic, Prague 6, Czech Republic

关键词: Phospholipase D;    Phosphorylation;    Cytoskeleton;    Brassica oleracea;    PLD;    phospholipase D;    PIP2;    phosphatidylinositol-4;    5-bisphosphate;    MALDI-TOF MS;    matrix-assisted laser desorption/ionization time-of-flight mass spectrometry;   

DOI  :  10.1016/S0014-5793(03)01093-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 BoPLDγ_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 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 PLDγ activity.

【 授权许可】

Unknown