1,2- sn-Diacylglycerol in plant cells: Product, substrate and regulator

• Published in: Plant physiology and biochemistry 1999-11, Vol.37 (11), p.795-808
• Main Authors: MIEGE, C, MARECHAL, E
• Format: Article
• Language: English
• Subjects: Biological and medical sciences; Cell biochemistry; Cell physiology; Diacylglycerol; diacylglycerol kinase; Fundamental and applied biological sciences. Psychology; MGDG synthase; monogalactosyldiacylglycerol; phosphatidate phosphatase; phosphatidic acid; Plant physiology and development; protein kinase C
• ISSN: 0981-9428; 1873-2690
• DOI: 10.1016/S0981-9428(99)00118-7

1,2- sn-Diacylglycerol (DAG) is a family of lipidic molecular species varying in the lengths and desaturation levels of acyl groups esterified at positions sn-1 and sn-2 of the glycerol backbone. In plant cells, DAG originating from plastid and from extraplastidial membranes have distinct molecular signatures, C18/C16 and C18/C18 structures, respectively. Under normal conditions, DAG is consumed nearly as fast as it is produced and is therefore a transient compound in the cell. In plants, DAG proved to be the most basic ingredient for cell membrane biogenesis and fat storage, but we still lack formal evidence to assert that DAG is also an intracellular messenger, as demonstrated for animals. From the biochemical and molecular comparisons of the best known DAG-manipulating proteins of prokaryotic and eukaryotic cells (phosphatidate phosphatases, diacylglycerol kinases, MGDG synthase, protein kinase C, etc.) this review aims to identify general rules driving DAG metabolism, and emphasizes its unique features in plant cells. DAG metabolism is an intricate network of local productions and utilizations: many isoenzymes can catalyse similar DAG modifications in distinct cell compartments or physiological processes. The enzymatic- or binding-specificity for DAG molecular species demonstrates that discrete DAG molecular subspecies fluxes are finely controlled (particularly for C18/C16 and C18/C18 structures in plastid membrane biogenesis). Eventually, this review stresses the diversity of structures and functioning of DAG-manipulating proteins. As a consequence, because DAG metabolism in plants is unique, the deciphering of genomic information cannot rely on homology searches using known prokaryotic, animal or yeast sequences, but requires sustained efforts in biochemical and molecular characterizations of plant DAG-manipulating proteins.