Activation of the β1 isozyme of phospholipase C by α subunits of the Gq class of G proteins
Abstract
Many hormones, neurotransmitters and growth factors, on binding to G protein-coupled receptors or receptors possessing tyrosine kinase activity, increase intracellular levels of the second messengers inositol 1,4,5-trisphosphate and 1,2-diacylglycerol. This is due to activation of phosphoinositide-specific phospholipase(s) C (PLC), the isozymes of which are classified into groups, alpha, beta, gamma and delta. The beta, gamma and delta groups themselves contain PLC isozymes which have both common and unique structural domains. Only the gamma 1 isozyme has been implicated in a signal transduction mechanism. This involves association with, and tyrosine phosphorylation by, the ligand-bound epidermal growth factor and platelet-derived growth factor receptors, probably by means of the PLC-gamma 1-specific src homology (SH2) domain. Because EGF receptor-mediated tyrosine phosphorylation of PLC-gamma 1 stimulates catalytic activity in vitro and G proteins have been implicated in the activation of PLC, we investigated which PLC isozymes are subject to G protein regulation. We have purified an activated G protein alpha subunit that stimulates partially purified phospholipase C and now report that this G protein specifically activates the beta 1 isozyme, but not the gamma 1 and delta 1 isozymes of phospholipase C. We also show that this protein is related to the Gq class of G protein alpha subunits.
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Gαq directly activates phospholipase C β.
“Gαq directly activates phospholipase C β [51].”
From G protein-coupled receptors function as cell membrane receptors for the steroid hormone 20-hydroxyecdysone (2020) · cites this paper as [51]
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- Authors
- Taylor, S. J., Chae, H. Z., Rhee, S. G., & Exton, J. H.
- Affiliations
- Howard Hughes Medical Institute (US)
- National Institutes of Health (US)
- ORCID
- Taylor, Stephen J.
- Venue
- Nature
- Published
- 1991-04
- Volume
- 350
- Issue
- 6318
- Pages
- 516-518
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W1565496454
- Cited by
- 780
- References
- 29
- Citations by year
- 2026: 5 · 2025: 5 · 2024: 3 · 2023: 7 · 2022: 8 · 2021: 7 · 2020: 5 · 2019: 5 · 2018: 3 · 2017: 4 · 2016: 5 · 2015: 8 · 2014: 3 · 2013: 10 · 2012: 12
- FWCI
- 41.62
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- 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 › Molecular Biology › Sphingolipid Metabolism and Signaling
- Keywords
- PLCB1, phospholipase C isozymes, PLCγ1, inositol 1,4,5-trisphosphate, diacylglycerol, second messengers, signal transduction, epidermal growth factor receptor, platelet-derived growth factor receptor, tyrosine phosphorylation, SH2 domain
- MeSH terms
- Animals, Binding Sites, Calcium, Cattle, Cell Membrane, Enzyme Activation, Isoenzymes, Liver, Molecular Weight, Type C Phospholipases, Receptors, Cell Surface, Tyrosine, Second Messenger Systems, Signal Transduction, Receptors, Platelet-Derived Growth Factor, Phosphotyrosine, GTP-Binding Proteins, Macromolecular Substances, ErbB Receptors
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