Stimulation of phospholipase Cβ by membrane interactions, interdomain movement, and G protein binding -: How many ways can you activate an enzyme?

被引:49
作者
Drin, Guillaume
Scarlata, Suzanne [1 ]
机构
[1] Inst Pharmacol Mol & Cellulaire, F-06560 Valbonne, France
[2] Univ Nice, F-06560 Valbonne, France
[3] SUNY Stony Brook, Dept Physiol & Biophys, Stony Brook, NY 11794 USA
关键词
PLC; G beta gamma; PH domain;
D O I
10.1016/j.cellsig.2007.04.006
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Signaling proteins are usually cornposed of one or more conserved structural domains. These domains are usually regulatory in nature by binding to specific activators or effectors, or species that regulate cellular location, etc. Inositol-specific mammalian phospholipase C (PLC) enzymes are multidomain proteins whose activities are controlled by regulators, such as G proteins, as well as membrane interactions. One of these domains has been found to bind membranes, regulators, and activate the catalytic region. The recently solved structure of a major region of PLC-beta 2 together with the structure of PLC-delta 1 and a wealth of biochemical studies poises the system towards an understanding of the mechanism through which their regulations occurs. (c) 2007 Elsevier Inc. All rights reserved.
引用
收藏
页码:1383 / 1392
页数:10
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