Functional and physical interactions of Syk family kinases with the Vav proto-oncogene product
Open accessAbstract
Syk family kinases are essential for lymphocyte development and activation. Therefore the identification of their direct effectors is of critical importance. Here, we report that Syk interacts in the yeast two-hybrid system with Vav, a proto-oncogene product exclusively expressed in hematopoietic cells. This interaction was direct, required the catalytic activity of Syk, the SH2 domain of Vav, and tyrosine residues in the linker domain of Syk. Vav also associated with Syk and Zap in antigen receptor-stimulated B or T cells, respectively. Functionally, Vav was phosphorylated by Syk family kinases both in vivo and in vitro. Furthermore, Syk and Vav cooperated to activate NF-AT synergistically. These results indicate that the interaction between Syk family kinases and Vav plays an important role in coupling immune recognition receptors to signaling pathways involved in lymphokine production.
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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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The SYK tyrosine kinase: A crucial player in diverse biological functions
Mócsai, A., Ruland, J., & Tybulewicz, V. L. J. (2010) · Nature Reviews Immunology · doi:10.1038/nri2765 · Cited by 1,368 · see citing works
Walliser, C., Hermkes, E., Schade, A., Wiese, S., Deinzer, J., Zapatka, M., Désiré, L., Mertens, D., Stilgenbauer, S., & Gierschik, P. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.746842 · Cited by 51 · see citing works
Rac2 Specificity in Macrophage Integrin Signaling
Pradip, D., Peng, X., & Durden, D. L. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m306491200 · Cited by 49 · see citing works
- Authors
- Deckert, M., Tartare-Deckert, S., Couture, C., Mustelin, T., & Altman, A.
- Affiliations
- La Jolla Institute for Immunology (US)
- Venue
- Immunity
- Publisher
- Elsevier BV
- Published
- 1996-12
- Volume
- 5
- Issue
- 6
- Pages
- 591-604
- ISSN
- 1074-7613 (ISSN-L)
- OpenAlex
- W2003319634
- Cited by
- 285
- References
- 0
- Citations by year
- 2025: 2 · 2024: 3 · 2023: 2 · 2022: 2 · 2021: 11 · 2020: 3 · 2019: 3 · 2018: 5 · 2017: 5 · 2016: 7 · 2015: 4 · 2014: 5 · 2013: 10 · 2012: 3
- FWCI
- 9.59
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Immunity (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Cancer Institute (CA 35299, R01CA035299)
- National Institute of General Medical Sciences (GM50819, R01GM050819)
- National Institute of Allergy and Infectious Diseases (R01AI035603, AI 35603)
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › T-cell and B-cell Immunology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Signaling Pathways in Disease
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
- Keywords
- Vav, ZAP, protein-protein interaction, SH2 domain, tyrosine phosphorylation, lymphocyte activation, antigen receptor signaling, B cells, T cells, hematopoietic cells, lymphokine production
- MeSH terms
- Syk Kinase, Proto-Oncogene Mas, B-Lymphocytes, Binding Sites, DNA-Binding Proteins, Enzyme Precursors, Humans, Lymphocyte Activation, Lymphocytes, Nuclear Proteins, Phosphorylation, Protein Binding, Protein-Tyrosine Kinases, Proto-Oncogene Proteins, Receptors, Antigen, B-Cell, Receptors, Antigen, T-Cell, Recombinant Fusion Proteins, T-Lymphocytes, Transcription Factors, Signal Transduction, Models, Immunological, Cell Cycle Proteins, src Homology Domains, Intracellular Signaling Peptides and Proteins, NFATC Transcription Factors, Proto-Oncogene Proteins c-vav, ZAP-70 Protein-Tyrosine Kinase
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