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Mechanism of B-Cell Receptor-Induced Phosphorylation and Activation of Phospholipase C-γ2

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Kim, Yeun Ju, Sekiya, Fujio, Poulin, Benoit, Bae, Yun Soo, Rhee, Sue Goo·2004·Molecular and Cellular Biology

DOI 10.1128/mcb.24.22.9986-9999.2004PMC PMC525462

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Abstract

Phospholipase C-gamma2 (PLC-gamma2) plays an important role in B-cell signaling. Phosphorylation of various tyrosine residues of PLC-gamma2 has been implicated in regulation of its lipase activity. With the use of antibodies specific for each of the putative phosphorylation sites, we have now shown that PLC-gamma2 is phosphorylated on Y753, Y759, and Y1217 in response to engagement of the B-cell receptor in Ramos cells, as well as in murine splenic B cells. In cells stimulated maximally via this receptor, the extent of phosphorylation of Y1217 was three times that of Y753 or of Y759. Stimulation of Jurkat T cells or platelets via their immunoreceptors also elicited phosphorylation of Y753 and Y759 but not that of Y1217. A basal level of phosphorylation of Y753 was apparent in unstimulated lymphocytes. The extent of phosphorylation of Y753 and Y759, but not that of Y1217, correlated with the lipase activity of PLC-gamma2. Examination of the effects of various pharmacological inhibitors and of RNA interference in Ramos cells suggested that Btk is largely, but not completely, responsible for phosphorylation of Y753 and Y759, whereas phosphorylation of Y1217 is independent of Btk. Finally, phosphorylation of Y1217 and that of Y753 and Y759 occurred on different PLC-gamma2 molecules.

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Authors: Kim, Y. J., Sekiya, F., Poulin, B., Bae, Y. S., & Rhee, S. G.
Affiliations: National Institutes of Health (US)
Ewha Womans University (KR)
Corresponding author: Rhee, Sue Goo
ORCID: Kim, Yeun Ju
Bae, Yun Soo
Rhee, Sue Goo
Venue: Molecular and Cellular Biology
Publisher: Informa UK Limited
Published: 2004-11
Volume: 24
Issue: 22
Pages: 9986-9999
ISSN: 0270-7306 (ISSN-L)
1098-5549
DOI: 10.1128/mcb.24.22.9986-9999.2004
PMC: PMC525462
OpenAlex: W2137816745
Cited by: 126
References: 55
Citations by year: 2026: 5 · 2025: 5 · 2024: 10 · 2023: 10 · 2022: 8 · 2021: 3 · 2020: 2 · 2019: 1 · 2018: 7 · 2017: 6 · 2016: 2 · 2015: 5 · 2014: 8 · 2013: 3 · 2012: 8
FWCI: 2.97
Type: journal article
Language: en
Open access: green
europepmc.org
Licence: journals.asm.org/non-commercial-tdm-license (tdm)
Locations: Molecular and Cellular Biology (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Life Sciences › Immunology and Microbiology › Immunology › T-cell and B-cell Immunology
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
Keywords: PLCγ2, B cell receptor signaling, tyrosine phosphorylation, Bruton's tyrosine kinase, lipase activity, Ramos cells, splenic B cells, T cell receptor signaling, RNA interference
MeSH terms: Agammaglobulinaemia Tyrosine Kinase, Amino Acid Sequence, Animals, Antibodies, B-Lymphocytes, Binding Sites, Cell Line, Enzyme Activation, Humans, Molecular Sequence Data, Type C Phospholipases, Phosphorylation, Protein-Tyrosine Kinases, Receptors, Antigen, B-Cell, Sequence Homology, Amino Acid, Jurkat Cells, RNA Interference, Mice, Phospholipase C gamma, In Vitro Techniques

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Mechanism of B-Cell Receptor-Induced Phosphorylation and Activation of Phospholipase C-γ2

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