Isozyme-specific stimulation of phospholipase C-γ2 by Rac GTPases
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The regulation of the two isoforms of phospholipase C-gamma, PLCgamma(1) and PLCgamma(2), by cell surface receptors involves protein tyrosine phosphorylation as well as interaction with adapter proteins and phosphatidylinositol 3,4,5-trisphosphate (PtdInsP(3)) generated by inositol phospholipid 3-kinases (PI3Ks). All three processes may lead to recruitment of the PLCgamma isozymes to the plasma membrane and/or stimulation of their catalytic activity. Recent evidence suggests that PLCgamma may also be regulated by Rho GTPases. In this study, PLCgamma(1) and PLCgamma(2) were reconstituted in intact cells and in a cell-free system with Rho GTPases to examine their influence on PLCgamma activity. PLCgamma(2), but not PLCgamma(1), was markedly activated in intact cells by constitutively active Rac1(G12V), Rac2(G12V), and Rac3(G12V) but not by Cdc42(G12V) and RhoA(G14V). The mechanism of PLCgamma(2) activation was apparently independent of phosphorylation of tyrosine residues known to be modified by PLCgamma(2)-activating protein-tyrosine kinases. Activation of PLCgamma(2) by Rac2(G12V) in intact cells coincided with a translocation of PLCgamma(2) from the soluble to the particulate fraction. PLCgamma isozyme-specific activation of PLCgamma(2) by Rac GTPases (Rac1 approximately Rac2 > Rac3), but not by Cdc42 or RhoA, was also observed in a cell-free system. Herein, activation of wild-type Rac GTPases with guanosine 5'-(3-O-thio)triphosphate caused a marked stimulation of PLCgamma(2) but had no effect on the activity of PLCgamma(1). PLCgamma(1) and PLCgamma(2) have previously been shown to be indiscriminately activated by PtdInsP(3) in vitro. Thus, the results suggest a novel mechanism of PLCgamma(2) activation by Rac GTPases involving neither protein tyrosine phosphorylation nor PI3K-mediated generation of PtdInsP(3).
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PLCγ2 is specifically activated by Rac GTPases by a mechanism independent of PLCγ2 tyrosine phosphorylation, but dependent on direct interaction of activated Rac with the bipartite split PH domain (spPH) juxtaposed between the two halves, X and Y, of the PLCγ2 catalytic domain.
“We have previously shown that PLC␥ 2 is specifically activated by Rac GTPases by a mechanism independent of PLC␥ 2 tyrosine phosphorylation, but dependent on the direct interaction of activated Rac with the bipartite split PH domain (spPH) juxtaposed between the two halves, X and Y, of the PLC␥ 2 catalytic domain (32,33).”
From The Phospholipase Cγ2 Mutants R665W and L845F Identified in Ibrutinib-resistant Chronic Lymphocytic Leukemia Patients Are Hypersensitive to the Rho GTPase Rac2 Protein (2016) · cites this paper as [32]
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- Authors
- Piechulek, T., Rehlen, T., Walliser, C., Vatter, P., Moepps, B., & Gierschik, P.
- Affiliations
- Universität Ulm (DE)
- Corresponding author
- Gierschik, Peter
- ORCID
- Gierschik, Peter
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2005-11
- Volume
- 280
- Issue
- 47
- Pages
- 38923-38931
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1993181949
- Cited by
- 80
- References
- 79
- Citations by year
- 2023: 3 · 2022: 3 · 2021: 2 · 2020: 3 · 2019: 2 · 2018: 3 · 2017: 1 · 2016: 4 · 2015: 10 · 2014: 6 · 2013: 3 · 2012: 9
- FWCI
- 1.64
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- 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 › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Sphingolipid Metabolism and Signaling
- Keywords
- PLCγ2, phospholipase C-gamma1, Rac GTPase, Rho GTPases, Cdc42, RhoA, Rac1, Rac2, RAC3, tyrosine phosphorylation, phosphatidylinositol 3,4,5-trisphosphate, plasma membrane translocation, GTP, cell-free reconstitution
- MeSH terms
- RAC2 GTP-Binding Protein, Animals, Cell Line, Cell Membrane, Cell-Free System, Chlorocebus aethiops, Enzyme Activation, Humans, Isoenzymes, Kinetics, Mutation, Recombinant Proteins, Transfection, COS Cells, rac GTP-Binding Proteins, rac1 GTP-Binding Protein, Phospholipase C gamma, In Vitro Techniques
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