Families of phosphoinositide-specific phospholipase C: structure and function

被引:180
作者
Katan, M [1 ]
机构
[1] Inst Canc Res, Chester Beatty Labs, CRC, Ctr Cell & Mol Biol, London SW3 6JB, England
来源
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR AND CELL BIOLOGY OF LIPIDS | 1998年 / 1436卷 / 1-2期
关键词
phosphoinositide-specific phospholipase C; phosphatidylinositol 4,5-bisphosphate; phosphatidylinositol 3,4,5-trisphosphate; inositol 1,3,5-trisphosphate; phospholipase C-gamma; phospholipase C-beta; phospholipase C-delta; PH domain; C2; domain; EF hand domain; SH2; SH3; catalysis; G-protein; tyrosine kinase; phosphatidylinositol; 3-kinase;
D O I
10.1016/S0005-2760(98)00125-8
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
A large number of extracellular signals stimulate hydrolysis of phosphatidylinositol 4,5-bisphosphate by phosphoinositide-specific phospholipase C (PI-PLC). PI-PLC isozymes have been found in a broad spectrum of organisms and although they have common catalytic properties, their regulation involves different signalling pathways, A number of recent studies provided an insight into domain organisation of PI-PLC isozymes and contributed towards better understanding of the structural basis for catalysis, cellular localisation and molecular changes that could underlie the process of their activation. (C) 1998 Elsevier Science B.V. All rights reserved.
引用
收藏
页码:5 / 17
页数:13
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