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Cell Signal. 2012 Jun;24(6):1333-43. doi: 10.1016/j.cellsig.2012.01.009. Epub 2012 Jan 20.

Role of phospholipase Cε in physiological phosphoinositide signaling networks.

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1
Department of Pharmacology and Physiology, University of Rochester School of Medicine, 601 Elmwood Ave, Rochester, NY 14642, USA. Alan_Smrcka@urmc.rochester.edu

Abstract

Receptor-initiated phospholipase C activation and generation of IP(3) and DAG are important common triggers for a diversity of signal transduction processes in many cell types. Contributing to this diversity is the existence and differential cellular and subcellular distribution of distinct phospholipase C isoforms with distinct regulatory properties. The recently identified PLCε enzyme is an isoform that is uniquely regulated by multiple upstream signals including ras-family GTP binding proteins as well as heterotrimeric G-proteins. In this review we will consider the well documented biochemical regulation of this isoform in the context of cell and whole animal physiology and in the context of other G protein-regulated PLC isoforms. These studies together reveal a surprisingly wide range of unexpected functions for PLCε in cellular signaling, physiology and disease.

PMID:
22286105
PMCID:
PMC3325758
DOI:
10.1016/j.cellsig.2012.01.009
[Indexed for MEDLINE]
Free PMC Article
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