PLC regulation: emerging pictures for molecular mechanisms

被引：135

作者：

Bunney, Tom D. ^{[1
]}

Katan, Matilda ^{[1
]}

机构：

[1] Inst Canc Res, Chester Beatty Labs, Sect Cell & Mol Biol, London SW3 6JB, England

来源：

TRENDS IN BIOCHEMICAL SCIENCES | 2011年 / 36卷 / 02期

关键词：

PHOSPHOLIPASE-C-GAMMA; PLECKSTRIN HOMOLOGY DOMAIN; TYROSINE KINASE; LIVING CELLS; CRYSTAL-STRUCTURE; RHO GTPASES; MEMBRANE; RECEPTOR; ACTIVATION; ISOZYMES;

D O I：

10.1016/j.tibs.2010.08.003

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：

Phosphoinositide-specific phospholipase C (PLC) enzymes are common signalling components linked to the activation of most cellular receptors. All PLC families are complex, modular, multi-domain proteins and together cover a broad spectrum of regulatory interactions, including direct binding to G protein subunits, small GTPases from Rho and Ras families, receptor and non-receptor tyrosine kinases and lipid components of cellular membranes. Recent structural determinations of PLC components and their complexes with regulatory proteins and direct mechanistic studies, together with earlier work, have provided the foundation to propose molecular mechanisms that stringently regulate PLC activity.

引用

页码：88 / 96

页数：9

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