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

被引:17
作者
Miège, C [1 ]
Maréchal, É [1 ]
机构
[1] Univ Grenoble 1, CEAG,CNRS,URA 576, Dept Biol Mol & Struct, Physiol Cellulaire Vegetale Lab, F-38054 Grenoble 9, France
关键词
diacylglycerol; diacylglycerol kinase; MGDG synthase; monogalactosyldiacylglycerol; phosphatidate phosphatase; phosphatidic acid; protein kinase C;
D O I
10.1016/S0981-9428(99)00118-7
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
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. (C) 1999 Editions scientifiques et medicales Elsevier SAS.
引用
收藏
页码:795 / 808
页数:14
相关论文
共 80 条
[1]   HUMAN BRAIN N-CHIMAERIN CDNA ENCODES A NOVEL PHORBOL ESTER RECEPTOR [J].
AHMED, S ;
KOZMA, R ;
MONFRIES, C ;
HALL, C ;
LIM, HH ;
SMITH, P ;
LIM, L .
BIOCHEMICAL JOURNAL, 1990, 272 (03) :767-773
[2]  
AHMED S, 1993, J BIOL CHEM, V268, P10709
[3]   THE CYSTEINE-RICH DOMAIN OF HUMAN PROTEINS, NEURONAL CHIMAERIN, PROTEIN-KINASE-C AND DIACYLGLYCEROL KINASE BINDS ZINC - EVIDENCE FOR THE INVOLVEMENT OF A ZINC-DEPENDENT STRUCTURE IN PHORBOL ESTER BINDING [J].
AHMED, S ;
KOZMA, R ;
LEE, J ;
MONFRIES, C ;
HARDEN, N ;
LIM, L .
BIOCHEMICAL JOURNAL, 1991, 280 :233-241
[4]  
[Anonymous], 1987, LIPIDS STRUCTURE FUN, DOI DOI 10.1016/B978-0-12-675409-4.50015-0
[5]   RICINOLEIC ACID BIOSYNTHESIS AND TRIACYLGLYCEROL ASSEMBLY IN MICROSOMAL PREPARATIONS FROM DEVELOPING CASTOR-BEAN (RICINUS-COMMUNIS) ENDOSPERM [J].
BAFOR, M ;
SMITH, MA ;
JONSSON, L ;
STOBART, K ;
STYMNE, S .
BIOCHEMICAL JOURNAL, 1991, 280 :507-514
[6]  
BHAT BG, 1994, J BIOL CHEM, V269, P13172
[7]  
BLOCK MA, 1983, J BIOL CHEM, V258, P3281
[8]   Phosphatidate phosphohydrolase and signal transduction [J].
Brindley, DN ;
Waggoner, DW .
CHEMISTRY AND PHYSICS OF LIPIDS, 1996, 80 (1-2) :45-57
[9]   Molecular cloning and characterization of a novel human diacylglycerol kinase zeta [J].
Bunting, M ;
Tang, W ;
Zimmerman, GA ;
McIntyre, TM ;
Prescott, SM .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1996, 271 (17) :10230-10236
[10]  
BURNS DJ, 1991, J BIOL CHEM, V266, P18330