Cutting Edge: Association of Phospholipase C-γ2 Src Homology 2 Domains with BLNK Is Critical for B Cell Antigen Receptor Signaling
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Abstract To explore the mechanism(s) by which phospholipase C (PLC)-γ2 participates in B cell Ag receptor (BCR) signaling, we have studied the function of PLC-γ2 mutants in B cells deficient in PLC-γ2. Mutation of the N-terminal Src homology 2 domain [SH2(N)] resulted in the complete loss of inositol 1,4,5-trisphosphate generation upon BCR engagement. A possible explanation for the SH2(N) requirement was provided by findings that this mutation abrogates the association of PLC-γ2 with an adaptor protein BLNK. Moreover, expression of a membrane-associated form (CD16/PLC-γ2) with SH2(N) mutation required coligation of BCR and CD16 for inositol 1,4,5-trisphosphate generation. Together, our results suggest a central role for the SH2(N) domain in directing PLC-γ2 into the close proximity of BCR signaling complex by its association with BLNK, whereby PLC-γ2 becomes tyrosine phosphorylated and thereby activated.
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The partner protein could be a RTK or a phosphotyrosine motif associated with an adaptor protein, such as LAT in T-cells, or BLNK in B-cells.
“The partner protein could be a RTK [84, 88] or a phosphotyrosine motif associated with an adaptor protein, such as LAT in T-cells [72], or BLNK in B-cells [89].”
From TREM2/PLCγ2 signalling in immune cells: function, structural insight, and potential therapeutic modulation (2021) · cites this paper as [89]
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Research works printed but not linked: 3
- Coggeshall, K. M., J. C. McHugh, and A. Altman. 1992. Predominant expression and activation-induced tyrosine phosphorylation of phospholipase C-␥2 in B lym- phocytes. Proc. Natl. Acad. Sci. USA 89:5660.
- Suh, P.-G., S. H. Ryu, K. H. Moon, H. W. Suh, and S. G. Rhee. 1988. Inositol phospholipid-specific phospholipase C: complete cDNA and protein sequences and sequence homology to tyrosine kinase-related oncogene products. Proc. Natl. Acad. Sci. USA 85:5419.
- Hashimoto, S., A. Iwamatsu, M. Ishiai, K. Okawa, T. Yamadori, M. Matsushita, Y. Baba, T. Kishimoto, T. Kurosaki, and S. Tsukada. 1999. Identification of the SH2 domain binding protein of Bruton's tyrosine kinase as BLNK: functional significance of Btk-SH2 domain in B cell antigen receptor-coupled calcium sig- naling. Blood. In press.
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- Authors
- Ishiai, M., Sugawara, H., Kurosaki, M., & Kurosaki, T.
- Affiliations
- Kansai Medical University (JP)
- Jichi Medical University (JP)
- Venue
- The Journal of Immunology
- Publisher
- Oxford University Press (OUP)
- Published
- 1999-08
- Volume
- 163
- Issue
- 4
- Pages
- 1746-1749
- ISSN
- 0022-1767 (ISSN-L)
- 1550-6606
- OpenAlex
- W4313422288
- Cited by
- 71
- References
- 0
- Citations by year
- 2022: 1 · 2021: 1 · 2017: 1 · 2016: 1 · 2014: 2 · 2013: 2 · 2012: 2
- FWCI
- 2.83
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The Journal of Immunology (publishedVersion)
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › T-cell and B-cell Immunology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
- Keywords
- PLCγ2, B cell receptor signaling, SH2 domain, BLNK, inositol 1,4,5-trisphosphate, CD16, tyrosine phosphorylation, adaptor proteins, B cell signaling
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