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Published on August 29, 2002; 10.1104/pp.004770


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Received February 22, 2002
Returned for revision April 2, 2002
Accepted June 21, 2002

Inositol Phospholipid Metabolism in Arabidopsis. Characterized and Putative Isoforms of Inositol Phospholipid Kinase and Phosphoinositide-Specific Phospholipase C Isoforms

Bernd Mueller-Roeber and Christophe Pical *

Universität Potsdam, Institut für Biochemie und Biologie, Abteilung Molekularbiologie, Karl-Liebknecht-Strasse 25, Haus 20, D-14476 Golm/Potsdam, Germany (B.M.-R.); and Lund University, Department of Plant Biochemistry, P.O. Box 124, SE-221 00 Lund, Sweden (C.P.)

* Corresponding author; email: christophe.pical{at}plantbio.lu.se.

Phosphoinositides (PIs) constitute a minor fraction of total cellular lipids in all eukaryotic cells. They fulfill many important functions through interaction with a wide range of cellular proteins. Members of distinct inositol lipid kinase families catalyze the synthesis of these phospholipids from phosphatidylinositol. The hydrolysis of PIs involves phosphatases and isoforms of PI-specific phospholipase C. Although our knowledge of the roles played by plant PIs is clearly limited at present, there is no doubt that they are involved in many physiological processes during plant growth and development. In this review, we concentrate on inositol lipid-metabolizing enzymes from the model plant Arabidopsis for which biochemical characterization data are available, namely the inositol lipid kinases and PI-specific phospholipase Cs. The biochemical properties and structure of characterized and genome-predicted isoforms are presented and compared with those of the animal enzymes to show that the plant enzymes have some features clearly unique to this kingdom.




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