Tyrosine phosphorylation of phospholipase C-gamma 1 induced by cross-linking of the high-affinity or low-affinity Fc receptor for IgG in U937 cells.

Liao, F; Shin, H S; Rhee, S G

doi:10.1073/pnas.89.8.3659

Cited by 144Monoclonal and Polyclonal Antibodies ResearchProtein Kinase Regulation and GTPase SignalingReceptor Mechanisms and Signaling

Tyrosine phosphorylation of phospholipase C-gamma 1 induced by cross-linking of the high-affinity or low-affinity Fc receptor for IgG in U937 cells.

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Liao, F, Shin, H S, Rhee, S G·1992·Proceedings of the National Academy of Sciences

DOI 10.1073/pnas.89.8.3659PMC PMC48928

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Abstract

The human monocytic cell line U937 possesses two classes of the IgG Fc receptor (Fc gamma R), a high-affinity 72-kDa Fc gamma R (Fc gamma RI) and a low-affinity 40-kDa Fc gamma R (Fc gamma RII). Cross-linking of either class of Fc gamma R in U937 cells elicits an increase in the concentration of free intracellular Ca2+. A rapid rise in the concentration of inositol 1,4,5-trisphosphate (Ins-1,4,5-P3) and of several other inositol phosphates derived from Ins-1,4,5-P3 was observed after cross-linking of Fc gamma Rs in U937 cells. This result suggests that Ins-1,4,5-P3, generated by the action of phospholipase C (PLC), acts as a second messenger by which Fc gamma Rs mobilize intracellular Ca2+ in U937 cells. The mechanism by which the cross-linking of Fc gamma Rs triggers activation of PLC was studied. Cross-linking of Fc gamma RI or Fc gamma RII resulted in a rapid and transient phosphorylation of PLC-gamma 1 on tyrosine residues. It has previously been shown that phosphorylation of PLC-gamma 1 on tyrosine residues activates its enzymatic activity in cells. Prior incubation of U937 cells with a protein tyrosine kinase inhibitor, herbimycin A, prevented the tyrosine phosphorylation of PLC-gamma 1 and the hydrolysis of phosphatidylinositol 4,5-bisphosphate induced by the cross-linking of Fc gamma Rs. Thus, Fc gamma RI and Fc gamma RII appear to be functionally coupled to a nonreceptor tyrosine kinase that phosphorylates PLC-gamma 1 after receptor cross-linking, thereby causing activation of PLC-gamma 1.

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4,5-PIP2 is the primary substrate of PLCγ, which becomes activated upon engagement of FcγRs.
“In addition to its role as a direct docking site for skeletal proteins, 4,5-PIP2 is also the primary substrate of phospholipase Cγ (PLCγ), which was shown to become activated upon engagement of FcγRs (Azzoni et al. 1992; Liao et al. 1992).”
From Localized Biphasic Changes in Phosphatidylinositol-4,5-Bisphosphate at Sites of Phagocytosis (2000) · cites this paper as Liao et al. 1992
The paper reports that cross-linking FcγRI or FcγRII in U937 cells leads to PLCγ1 phosphorylation and hydrolysis of phosphatidylinositol 4,5-bisphosphate (abstract, p. 3659). This supports receptor-linked PLCγ activity and identifies 4,5-PIP2 as a substrate, but the passage does not establish that it is PLCγ’s primary substrate. (LLM, conf=0.84)
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Authors: Liao, F., Shin, H. S., & Rhee, S. G.
Affiliations: Johns Hopkins University (US)
ORCID: Shin, H S
Rhee, S G
Venue: Proceedings of the National Academy of Sciences
Publisher: National Academy of Sciences
Published: 1992-04-15
Volume: 89
Issue: 8
Pages: 3659-3663
ISSN: 0027-8424 (ISSN-L)
1091-6490
DOI: 10.1073/pnas.89.8.3659
PMC: PMC48928
OpenAlex: W2035439001
Cited by: 144
References: 35
Citations by year: 2025: 2 · 2024: 1 · 2023: 2 · 2021: 2 · 2020: 1 · 2019: 1 · 2018: 2 · 2017: 2 · 2016: 6 · 2014: 3 · 2013: 5 · 2012: 5
FWCI: 19.75
Type: journal article
Language: en
Open access: green
europepmc.org
Locations: Proceedings of the National Academy of Sciences (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Topics: Health Sciences › Medicine › Radiology, Nuclear Medicine and Imaging › Monoclonal and Polyclonal Antibodies Research
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
Keywords: phospholipase C-gamma1, tyrosine phosphorylation, Fc gamma receptor I, Fc gamma receptor II, U937 cells, calcium mobilization, inositol 1,4,5-trisphosphate, inositol phosphates, non-receptor tyrosine kinase, herbimycin A, phosphatidylinositol 4,5-bisphosphate hydrolysis, second messenger signaling, monocytic cells
MeSH terms: Antigens, Differentiation, Arsenicals, Calcium, Cell Line, Cross-Linking Reagents, Humans, Immunoglobulin G, Inositol Phosphates, Kinetics, Phosphates, Phosphatidylinositols, Type C Phospholipases, Phosphorylation, Receptors, Fc, Tyrosine, Inositol 1,4,5-Trisphosphate, Receptors, IgG, Phosphotyrosine, Phosphatidylinositol 4,5-Diphosphate

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Tyrosine phosphorylation of phospholipase C-gamma 1 induced by cross-linking of the high-affinity or low-affinity Fc receptor for IgG in U937 cells.

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