4.6 Review

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

Journal

CELLULAR SIGNALLING
Volume 19, Issue 7, Pages 1383-1392

Publisher

ELSEVIER SCIENCE INC
DOI: 10.1016/j.cellsig.2007.04.006

Keywords

PLC; G beta gamma; PH domain

Categories

Funding

  1. NIGMS NIH HHS [R01 GM053132-10, R01 GM053132, GM 053132] Funding Source: Medline

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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.

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