B Cell Receptor-Mediated Syk-Independent Activation of Phosphatidylinositol 3-Kinase, Ras, and Mitogen-Activated Protein Kinase Pathways

Yokozeki, Takeaki; Adler, Kristin; Lankar, Danielle; Bonnerot, Christian

doi:10.4049/jimmunol.171.3.1328

Cited by 31T-cell and B-cell ImmunologyNF-κB Signaling PathwaysProtein Kinase Regulation and GTPase Signaling

B Cell Receptor-Mediated Syk-Independent Activation of Phosphatidylinositol 3-Kinase, Ras, and Mitogen-Activated Protein Kinase Pathways

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Yokozeki, Takeaki, Adler, Kristin, Lankar, Danielle, Bonnerot, Christian·2003·The Journal of Immunology

DOI 10.4049/jimmunol.171.3.1328

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Abstract

The Syk tyrosine kinase is a key molecule in the development of the B cell lineage and the activation of B lymphocytes after Ag recognition by the B cell Ag receptor (BCR). Several genetic studies with chicken B cells have reported that the recruitment of Syk by BCR is essential for activation of a cascade of signaling molecules including phosphatidylinositol 3-kinase, mitogen-activated protein kinases, Ras signaling pathways, phospholipase C-γ2 activation, and calcium mobilization. The identification of a Syk-deficient mouse IIA1.6/A20 B cell line provided us the opportunity to investigate Syk-mediated signaling in mouse. Surprisingly, phosphatidylinositol 3-kinase, Ras, and mitogen-activated protein kinases were activated upon BCR cross-linking in these Syk-deficient mouse B cells, whereas, as expected from results obtained in chicken B cells, phospholipase C-γ2 activation and calcium mobilization were impaired as well as the NF-κB pathway. These results indicate that BCR signaling is not strictly dependent on Syk expression in mouse IIA1.6/A20 B cells. Thus, B lymphocyte activation may be initiated by Syk-dependent and Syk-independent signaling cascades.

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PLCγ2 activation results in activation of phospholipase D and cell spreading, and brings on Erk signaling.
“In addition to the production of IP3, DAG, and calcium flux, PLCγ2 activation results in activation of phospholipase D and cell spreading (12, 13, 14, 15, 16, 17), bringing on other vital cell signaling processes such as Erk (18).”
From The role of PLCγ2 in immunological disorders, cancer, and neurodegeneration (2021) · cites this paper as [15]
Citation 18 is attached to the Erk-signaling clause, not the phospholipase D or cell-spreading claims cited to references 12–17. The Discussion suggests that the Syk-dependent PLCγ2 pathway cooperates with Ras and PI3K in regulating ERK, but the section on MAPK activation reports strong early ERK2 activation even in Syk-deficient cells unable to activate PLCγ2. The source therefore supports a possible PLCγ2 contribution, not an unqualified claim that PLCγ2 activation brings on Erk signaling. (LLM, conf=0.86)
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Authors: Yokozeki, T., Adler, K., Lankar, D., & Bonnerot, C.
Affiliations: Inserm (FR)
Venue: The Journal of Immunology
Publisher: Oxford University Press (OUP)
Published: 2003-08-01
Volume: 171
Issue: 3
Pages: 1328-1335
ISSN: 0022-1767 (ISSN-L)
1550-6606
DOI: 10.4049/jimmunol.171.3.1328
OpenAlex: W1572385475
Cited by: 31
References: 60
Citations by year: 2021: 2 · 2020: 2 · 2019: 1 · 2018: 1 · 2017: 1 · 2016: 1 · 2015: 2 · 2014: 2 · 2012: 1
FWCI: 0.99
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: academic.oup.com/pages/standard-publication-reuse-rights (vor)
Locations: The Journal of Immunology (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Immunology and Microbiology › Immunology › T-cell and B-cell Immunology
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Keywords: B cell receptor signaling, Syk, phosphatidylinositol 3-kinase, Ras signaling, mitogen-activated protein kinase, PLCγ2, calcium mobilization, NF-κB signaling, B cell activation
MeSH terms: Syk Kinase, Amino Acid Sequence, Animals, Calcium, Clone Cells, Enzyme Activation, Enzyme Precursors, Interleukin-2, Lymphocyte Activation, Molecular Sequence Data, Type C Phospholipases, Phosphorylation, Protein-Tyrosine Kinases, Receptors, Antigen, B-Cell, Tumor Cells, Cultured, Tyrosine, Signal Transduction, NF-kappa B, ras Proteins, Antigens, CD19, Phosphatidylinositol 3-Kinases, Mitogen-Activated Protein Kinases, MAP Kinase Signaling System, Intracellular Signaling Peptides and Proteins, Mice, Phospholipase C gamma

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B Cell Receptor-Mediated Syk-Independent Activation of Phosphatidylinositol 3-Kinase, Ras, and Mitogen-Activated Protein Kinase Pathways

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