The DOI matches its Crossref record; 56 of the 56 references it cites were found in a registry or an index.
A role for Bruton's tyrosine kinase in B cell antigen receptor-mediated activation of phospholipase C-gamma 2.
Open accessAbstract
Defects in the gene encoding Bruton's tyrosine kinase (Btk) result in a disease called X-linked agammaglobulinemia, in which there is a profound decrease of mature B cells due to a block in B cell development. Recent studies have shown that Btk is tyrosine phosphorylated and activated upon B cell antigen receptor (BCR) stimulation. To elucidate the functions of this kinase, we examined BCR signaling of DT40 B cells deficient in Btk. Tyrosine phosphorylation of phospholipase C (PLC)-gamma 2 upon receptor stimulation was significantly reduced in the mutant cells, leading to the loss of both BCR-coupled phosphatidylinositol hydrolysis and calcium mobilization. Pleckstrin homology and Src-homology 2 domains of Btk were required for PLC-gamma 2 activation. Since Syk is also required for the BCR-induced PLC-gamma 2 activation, our findings indicate that PLC-gamma 2 activation is regulated by Btk and Syk through their concerted actions.
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Cited by
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THE HIGH-AFFINITY I g E RECEPTOR (FcεRI): From Physiology to Pathology
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B cell antigen receptor signaling 101
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Metadata
- Authors
- Takata, M., & Kurosaki, T.
- Venue
- The Journal of experimental medicine
- Publisher
- Rockefeller University Press
- Published
- 1996-07-01
- Volume
- 184
- Issue
- 1
- Pages
- 31-40
- ISSN
- 0022-1007 (ISSN-L)
- 1540-9538
- OpenAlex
- W2035277099
- Cited by
- 484
- References
- 56
- FWCI
- 15.26
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Takata, M., & Kurosaki, T. (1996). A role for Bruton's tyrosine kinase in B cell antigen receptor-mediated activation of phospholipase C-gamma 2. The Journal of experimental medicine. https://doi.org/10.1084/jem.184.1.31
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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