The SH3 Domain of Bruton's Tyrosine Kinase Interacts with Vav, Sam68 and EWS
Abstract
Bruton tyrosine kinase (BTK) is a cytoplasmic protein tyrosine kinase which controls crucial steps of differentiation of B lymphocytes. Mutations affecting either the PH, SH3, SH2 or kinase domain of BTK all give rise to X linked agammaglobulinaemia (XLA) in humans. In this study, the authors report that the BTK-SH3 domain binds to a set of proteins expressed in pro-B, pre-B and B cell lines. Three of them were characterized as Vav, Sam68 and EWS. The authors show that a Pro-->Leu substitution in a region of the SH3 domain, which is deleted in an XLA patient, is sufficient to abolish BTK-SH3 binding potential. The authors also report that several of the BTK-SH3 binding proteins, including Sam68, EWS and Vav, are tyrosine phosphorylated in conditions that also promote BTK kinase activity. For EWS and Sam68 this tyrosine phosphorylation was cell cycle dependent.
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Several elements of the canonical BCR signaling cascade, e.g. Syk, Btk, and BLNK, are known to physically interact with and activate the Rac activator Vav, by processes not necessarily involving the protein kinase activity of Btk.
“Thus, several elements of the canonical BCR signaling cascade, e.g.Syk (50), Btk (51), and BLNK (52,53), are known to physically interact with and activate the Rac activator Vav, by processes not necessarily involving the protein kinase activity of Btk.”
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- Authors
- GUINAMARD, R., FOUGEREAU, M., & SECKINGER, P.
- Affiliations
- Centre National de la Recherche Scientifique (FR)
- ORCID
- GUINAMARD, R.
- Venue
- Scandinavian Journal of Immunology
- Publisher
- Wiley
- Published
- 1997-06
- Volume
- 45
- Issue
- 6
- Pages
- 587-595
- ISSN
- 0300-9475 (ISSN-L)
- 1365-3083
- OpenAlex
- W2088741694
- Cited by
- 76
- References
- 0
- Citations by year
- 2025: 1 · 2024: 2 · 2022: 3 · 2017: 2 · 2016: 2 · 2015: 2 · 2013: 3 · 2012: 1
- FWCI
- 2.76
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Scandinavian Journal of Immunology (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion)
- Funders
- Institut National de la Santé et de la Recherche Médicale
- Centre National de la Recherche Scientifique
- Institut Universitaire de France
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › Immunodeficiency and Autoimmune Disorders
- 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
- Keywords
- Bruton's tyrosine kinase, SH3 domain, Vav, Sam68, Ewing sarcoma protein, protein-protein interaction, X-linked agammaglobulinemia, tyrosine phosphorylation, B cell differentiation, pro-B cells, pre-B cells, cell cycle regulation, kinase activity
- MeSH terms
- Agammaglobulinaemia Tyrosine Kinase, Amino Acid Sequence, B-Lymphocytes, Cell Cycle, Cell Line, DNA-Binding Proteins, Humans, Molecular Sequence Data, Mutation, Phosphoproteins, Phosphorylation, Protein Binding, Protein-Tyrosine Kinases, Proto-Oncogene Proteins, Ribonucleoproteins, Sarcoma, Ewing, Tyrosine, RNA-Binding Proteins, Cell Cycle Proteins, src Homology Domains, Heterogeneous-Nuclear Ribonucleoproteins, RNA-Binding Protein EWS, Adaptor Proteins, Signal Transducing, Proto-Oncogene Proteins c-vav
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