2Plant Biotechnology Institute, National Research Council of Canada, 110 Gymnasium Place, Saskatoon, SK, S7N 0W9, Canada; E-mail: Kateryna.Nokhrina@nrc-cnrc.gc.ca
3Institute of Biophysics and Cell Engineering, National Academy of Sciences of Belarus, ul. Akademicheskaya 27, 220072 Minsk, Belarus; E-mail: firstname.lastname@example.org
4Institute of Experimental Botany, Academy of Sciences of the Czech Republic, Rozvojova 263, 16502 Prague 6, Czech Republic; fax: +420 (225) 106-456, E-mail: email@example.com
5Institute of Plant Physiology, Russian Academy of Sciences, ul. Botanicheskaya 35, 127276 Moscow, Russia; E-mail: firstname.lastname@example.org
* To whom correspondence should be addressed.
Received February 1, 2011; Revision received March 23, 2011
Phospholipase D (PLD) catalyzes hydrolysis of phospholipids with production of phosphatidic acid, which often acts as secondary messenger of transduction of intracellular signals. This review summarizes data of leading laboratories on specific features of organization and regulation of PLD activity in plant and animal cells. The main structural domains of PLD (C2, PX, PH), the active site, and other functionally important parts of the enzyme are discussed. Regulatory mechanisms of PLD activity are characterized in detail. Studies associated with molecular design, analysis, and synthesis of new nontoxic substances capable of inhibiting different PLD isoenzymes in vivo are shown to be promising for biotechnology and medicine.
KEY WORDS: phospholipase D, domains, calcium, lipids, G-proteins, protein kinases, protein–protein interactions