Structural and mechanistic features of phospholipases C: Effectors of inositol phospholipid-mediated signal transduction

被引:38
作者
James, SR
Downes, CP
机构
[1] Department of Biochemistry, Medical Sciences Institute, University of Dundee, Dundee
关键词
phospholipases C; signal transduction; effectors of inositol phospholipid-mediated;
D O I
10.1016/S0898-6568(96)00175-1
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
The production of the intracellular second messengers inositol (1,4,5)-trisphosphate (InsP(3)) and sn 1,2-diacylglycerol (DG) in response to a wide variety of extracellular primary messengers is achieved by an extended family of inositol phospholipid phosphodiesterases termed phospholipases C (PLC, E.C. 3.1.4.11). This family has been the subject of extensive research and it is clear that the different isoenzymes exhibit some common characteristics (e.g., interactions with substrates) and other distinctive features (e.g., modes of regulation). The recent description of the X-ray crystal structure of a mammalian PLC has served to clarify much about the behaviour of the PLCs, emphasising the ''modular'' structure of these enzymes. The main focus of this review will concern the specific adaptations of PLC molecules which make them efficient lipid-metabolising enzymes. We also describe what is known about how these enzymes interact with their lipid substrates, which will serve as a basis for considering how PLCs may be activated. (C) 1997 Elsevier Science Inc.
引用
收藏
页码:329 / 336
页数:8
相关论文
共 87 条
[1]  
BAHK YY, 1994, J BIOL CHEM, V269, P8240
[2]   Structure of bacterial luciferase [J].
Baldwin, TO ;
Christopher, JA ;
Raushel, FM ;
Sinclair, JF ;
Ziegler, MM ;
Fisher, AJ ;
Rayment, I .
CURRENT OPINION IN STRUCTURAL BIOLOGY, 1995, 5 (06) :798-809
[3]   STRUCTURE OF CHICKEN MUSCLE TRIOSE PHOSPHATE ISOMERASE DETERMINED CRYSTALLOGRAPHICALLY AT 2.5A RESOLUTION USING AMINO-ACID SEQUENCE DATA [J].
BANNER, DW ;
BLOOMER, AC ;
PETSKO, GA ;
PHILLIPS, DC ;
POGSON, CI ;
WILSON, IA ;
CORRAN, PH ;
FURTH, AJ ;
MILMAN, JD ;
OFFORD, RE ;
PRIDDLE, JD ;
WALEY, SG .
NATURE, 1975, 255 (5510) :609-614
[4]   INTERFACIAL CATALYSIS BY PHOSPHOINOSITIDE 3'-HYDROXYKINASE [J].
BARNETT, SF ;
LEDDER, LM ;
STIRDIVANT, SM ;
AHERN, J ;
CONROY, RR ;
HEIMBROOK, DC .
BIOCHEMISTRY, 1995, 34 (43) :14254-14262
[5]   PHOSPHOLIPASE C-BETA-1 IS A GTPASE-ACTIVATING PROTEIN FOR GQ/11, ITS PHYSIOLOGICAL REGULATOR [J].
BERSTEIN, G ;
BLANK, JL ;
JHON, DY ;
EXTON, JH ;
RHEE, SG ;
ROSS, EM .
CELL, 1992, 70 (03) :411-418
[6]   Regulation of phospholipase C-beta 1 by G(q) and m1 muscarinic cholinergic receptor - Steady-state balance of receptor-mediated activation and GTPase-activating protein-promoted deactivation [J].
Biddlecome, GH ;
Berstein, G ;
Ross, EM .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1996, 271 (14) :7999-8007
[7]  
BLANK JL, 1991, J BIOL CHEM, V266, P18206
[8]   EFFECT OF MONOLAYER SURFACE PRESSURE ON THE ACTIVITIES OF PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE-C-BETA-1, PHOSPHOLIPASE-C-GAMMA-1, AND PHOSPHOLIPASE-C-DELTA-1 [J].
BOGUSLAVSKY, V ;
REBECCHI, M ;
MORRIS, AJ ;
JHON, DY ;
RHEE, SG ;
MCLAUGHLIN, S .
BIOCHEMISTRY, 1994, 33 (10) :3032-3037
[9]   A SERINE PROTEASE TRIAD FORMS THE CATALYTIC CENTER OF A TRIACYLGLYCEROL LIPASE [J].
BRADY, L ;
BRZOZOWSKI, AM ;
DEREWENDA, ZS ;
DODSON, E ;
DODSON, G ;
TOLLEY, S ;
TURKENBURG, JP ;
CHRISTIANSEN, L ;
HUGEJENSEN, B ;
NORSKOV, L ;
THIM, L ;
MENGE, U .
NATURE, 1990, 343 (6260) :767-770
[10]  
BUXEDA RJ, 1991, J BIOL CHEM, V266, P13859