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Phospholipase C (PLC) β and ε enzymes hydrolyze phosphatidylinositol (PI) lipids in response to direct interactions with heterotrimeric G protein subunits and small GTPases, which are activated downstream of G protein-coupled receptors (GPCRs) and receptor tyrosine kinases (RTKs). PI hydrolysis generates second messengers that increase the intracellular Ca2+ concentration and activate protein kinase C (PKC), thereby regulating numerous physiological processes. PLCβ and PLCε share a highly conserved core required for lipase activity, but use different strategies and structural elements to autoinhibit basal activity, bind membranes, and engage G protein activators. In this review, we discuss recent structural insights into these enzymes and the implications for how they engage membranes alone or in complex with their G protein regulators. Copyright © 2021 Elsevier B.V. All rights reserved.

Citation

Kaushik Muralidharan, Michelle M Van Camp, Angeline M Lyon. Structure and regulation of phospholipase Cβ and ε at the membrane. Chemistry and physics of lipids. 2021 Mar;235:105050

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PMID: 33422547

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