The Phospholipase C Isozymes and Their Regulation

Gresset, Aurelie; Sondek, John; Harden, T. Kendall

doi:10.1007/978-94-007-3012-0_3

Cited by 197Protein Kinase Regulation and GTPase SignalingReceptor Mechanisms and SignalingCellular transport and secretion

The Phospholipase C Isozymes and Their Regulation

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Gresset, Aurelie, Sondek, John, Harden, T. Kendall·2012·Subcellular Biochemistry

DOI 10.1007/978-94-007-3012-0_3PMC PMC3638883

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Abstract

The physiological effects of many extracellular neurotransmitters, hormones, growth factors, and other stimuli are mediated by receptor-promoted activation of phospholipase C (PLC) and consequential activation of inositol lipid signaling pathways. These signaling responses include the classically described conversion of phosphatidylinositol(4,5)P(2) to the Ca(2+)-mobilizing second messenger inositol(1,4,5)P(3) and the protein kinase C-activating second messenger diacylglycerol as well as alterations in membrane association or activity of many proteins that harbor phosphoinositide binding domains. The 13 mammalian PLCs elaborate a minimal catalytic core typified by PLC-d to confer multiple modes of regulation of lipase activity. PLC-b isozymes are activated by Gaq- and Gbg-subunits of heterotrimeric G proteins, and activation of PLC-g isozymes occurs through phosphorylation promoted by receptor and non-receptor tyrosine kinases. PLC-e and certain members of the PLC-b and PLC-g subclasses of isozymes are activated by direct binding of small G proteins of the Ras, Rho, and Rac subfamilies of GTPases. Recent high resolution three dimensional structures together with biochemical studies have illustrated that the X/Y linker region of the catalytic core mediates autoinhibition of most if not all PLC isozymes. Activation occurs as a consequence of removal of this autoinhibition.

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Mammalian PLC enzymes that use phosphoinositides, preferentially PI(4,5)P2, are grouped into six families (β, γ, δ, ε, ζ and η).
“In mammals, PLC enzymes that use phosphoinositides (preferentially PI(4,5)P2) as their substrates have been grouped into six families (β, γ, δ, ε, ζ and η).”
From Phosphatidylinositol(4,5)bisphosphate: diverse functions at the plasma membrane (2020) · cites this paper as [30]
Signalling connectivity is best defined for GPCRs and PLCβ isoforms via G-protein α and βγ subunits, and for RTKs and tyrosine kinases linked to ITAM-associated receptors that activate PLC enzymes by direct phosphorylation.
“Overall, the signalling connectivity remains best defined for the G-protein coupled receptors (GPCRs) and PLCβ isoforms, mediated by the α and βγ subunits of G-proteins, and for the RTKs and tyrosine kinases linked to immunoreceptor tyrosine-based activation motif (ITAM)-associated receptors, that activate PLC enzymes by direct phosphorylation.”
From Phosphatidylinositol(4,5)bisphosphate: diverse functions at the plasma membrane (2020) · cites this paper as [30]
There are thirteen PLCs in mammals: four PLCβ, two PLCγ, three PLCδ, one PLCε, one PLCζ and two PLCη.
“Within each family are multiple members: four PLCβ (1–4), two PLCγ (1 and 2), three PLCδ (1, 3, 4), one PLCε, one PLCζ and two PLCη (1 and 2) making thirteen PLCs in total (reviewed in [27–33]) (Figure 3A).”
From Phosphatidylinositol(4,5)bisphosphate: diverse functions at the plasma membrane (2020) · cites this paper as [30]

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Aberrant accumulation of phospholipase C-delta in Alzheimer brains.
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Gα12/13- and Rho-Dependent Activation of Phospholipase C-ϵ by Lysophosphatidic Acid and Thrombin Receptors
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Carboxyl-terminal Fragments of Phospholipase C-β1 with Intrinsic Gq GTPase-activating Protein (GAP) Activity
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Mutations within a highly conserved sequence present in the X region of phosphoinositide-specific phospholipase C-δ1
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The amino-terminal Src homology 2 domain of phospholipase C gamma 1 is essential for TCR-induced tyrosine phosphorylation of phospholipase C gamma 1.
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The Role of X/Y Linker Region and N-terminal EF-hand Domain in Nuclear Translocation and Ca2+ Oscillation-inducing Activities of Phospholipase Cζ, a Mammalian Egg-activating Factor
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Rac regulates its effector phospholipase Cγ2 through interaction with a split pleckstrin homology domain
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Mutations in the Carboxyl-terminal Domain of Phospholipase C-β1 Delineate the Dimer Interface and a Potential GαqInteraction Site
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The Amino-Terminal Src Homology 2 Domain of Phospholipase Cγ1 Is Essential for TCR-Induced Tyrosine Phosphorylation of Phospholipase Cγ1
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A receptor and G-protein-regulated polyphosphoinositide-specific phospholipase C from turkey erythrocytes. II. P2Y-purinergic receptor and G-protein-mediated regulation of the purified enzyme reconstituted with turkey erythrocyte ghosts.
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Phospholipase C isozymes as effectors of Ras superfamily GTPases
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Phospholipase C δ-type consists of three isozymes: bovine PLCδ2 is a homologue of human/mouse PLCδ4
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ANG II-induced tyrosine phosphorylation stimulates phospholipase C-gamma 1 and Cl-channels in mesangial cells
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Bradykinin Stimulates the Tyrosine Phosphorylation and Bradykinin B2 Receptor Association of Phospholipase Cγ1 in Vascular Endothelial Cells
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Lack of phospholipase C-δ1 induces skin inflammation
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Dual Activation of Phospholipase C-ϵ by Rho and Ras GTPases
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Identification of a Region at the N-Terminus of Phospholipase C-β3 That Interacts with G Protein βγ Subunits
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Inositides in the nucleus: presence and characterisation of the isozymes of phospholipase β family in NIH 3T3 cells
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Differential Regulation of Phospholipase C-β2 Activity and Membrane Interaction by Gαq, Gβ1γ2, and Rac2
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Identification of residues in the beta platelet-derived growth factor receptor that confer specificity for binding to phospholipase C-gamma 1.
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Activation of Human Phospholipase C-η2 by Gβγ
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Phospholipase C-δ1 Expression Is Linked to Proliferation, DNA Synthesis, and Cyclin E Levels
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Differential Roles of the Src Homology 2 Domains of Phospholipase C-γ1 (PLC-γ1) in Platelet-derived Growth Factor-induced Activation of PLC-γ1 in Intact Cells
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Enhanced phospholipase C-gamma1 activity produced by association of independently expressed X and Y domain polypeptides.
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Phospholipase C-γ1 and phospholipase C-γ2 are substrates of the B cell antigen receptor associated protein tyrosine kinase
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Reassembly of Phospholipase C-β2 from Separated Domains
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A unique isoform of phospholipase Cβ4 highly expressed in the cerebellum and eye
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Limited proteolysis of phospholipase C-γ 1 indicates stable association of X and Y domains with enhanced catalytic activity
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Phospholipase C-eta2 is highly expressed in the habenula and retina
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Membrane Environment Exerts an Important Influence on Rac-Mediated Activation of Phospholipase Cγ2
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Molecular cloning of the plc1+ gene of Schizosaccharomyces pombe, which encodes a putative phosphoinositide‐specific phospholipase C
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Abnormal accumulation of phospholipase C-δ in filamentous inclusions of human neurodegenerative diseases
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Equivocal, explicit and emergent actions of PKC isoforms in cancer
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The endocannabinoidome in neuropsychiatry: Opportunities and potential risks
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Membrane-induced Allosteric Control of Phospholipase C-β Isozymes
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Atypical activation of the G protein Gαq by the oncogenic mutation Q209P
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PLCE1 promotes myocardial ischemia–reperfusion injury in H/R H9c2 cells and I/R rats by promoting inflammation
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Search and Subvert: Minimalist Bacterial Phosphatidylinositol-Specific Phospholipase C Enzymes
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Authors: Gresset, A., Sondek, J., & Harden, T. K.
Affiliations: University of North Carolina at Chapel Hill (US)
Corresponding author: Harden, T. Kendall
ORCID: Sondek, John
Venue: Subcellular Biochemistry
Publisher: Springer Netherlands
Published: 2012
Volume: 58
Pages: 61-94
ISSN: 0306-0225 (ISSN-L)
DOI: 10.1007/978-94-007-3012-0_3
PMC: PMC3638883
OpenAlex: W199111168
Cited by: 196
References: 208
Citations by year: 2026: 8 · 2025: 14 · 2024: 12 · 2023: 24 · 2022: 21 · 2021: 21 · 2020: 18 · 2019: 15 · 2018: 14 · 2017: 8 · 2016: 7 · 2015: 12 · 2014: 11 · 2013: 8 · 2012: 3
FWCI: 18.57
Type: book chapter
Language: en
Open access: green
europepmc.org
Locations: Sub-cellular biochemistry/Subcellular biochemistry (publishedVersion)
PubMed (publishedVersion)
Europe PMC (PubMed Central) (acceptedVersion)
PubMed Central (acceptedVersion)
Funders: National Institute of General Medical Sciences (R01GM057391)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
Keywords: phospholipase C isozymes, inositol lipid signaling, phosphatidylinositol 4,5-bisphosphate, diacylglycerol, protein kinase C, heterotrimeric G proteins, tyrosine kinase phosphorylation, small GTPases, Ras, Rho, Rac, autoinhibition, catalytic core, calcium signaling
MeSH terms: Animals, Diglycerides, Enzyme Activation, Eukaryotic Cells, Gene Expression Regulation, Humans, Isoenzymes, Models, Molecular, Type C Phospholipases, Phosphorylation, Second Messenger Systems, Inositol 1,4,5-Trisphosphate, Protein Structure, Secondary, Protein Structure, Tertiary, Phosphatidylinositol 4,5-Diphosphate, Heterotrimeric GTP-Binding Proteins

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The Phospholipase C Isozymes and Their Regulation

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