ArticleProceedings of the National Academy of Sciences of the United States of America2010
Syk is a dual-specificity kinase that self-regulates the signal output from the B-cell antigen receptor.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
What it found
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Who cites it
27 citing papers in PubMed, 51 citations in OpenAlex.
- Targeting myeloid cells to improve cancer immune therapy.Frontiers in immunology · 2025Review
- Syk-dependent homologous recombination activation promotes cancer resistance to DNA targeted therapy.Drug resistance updates : reviews and commentaries in antimicrobial and anticancer chemotherapy · 2024Article
- T-independent B-cell effect of agents associated with swine grower-finisher diarrhea.Veterinary research communications · 2024Article
- The ion channel TRPV5 regulates B-cell signaling and activation.Frontiers in immunology · 2024Article
- Intestinal B cells license metabolic T-cell activation in NASH microbiota/antigen-independently and contribute to fibrosis by IgA-FcR signalling.Journal of hepatology · 2023Article
- Tumor cell SYK expression modulates the tumor immune microenvironment composition in human cancer via TNF-α dependent signaling.Journal for immunotherapy of cancer · 2022Article
- Development of New Drugs for Autoimmune Hemolytic Anemia.Pharmaceutics · 2022Review
- The transmembrane adapter SCIMP recruits tyrosine kinase Syk to phosphorylate Toll-like receptors to mediate selective inflammatory outputs.The Journal of biological chemistry · 2022Article
- Constitutively Activated DAP12 Induces Functional Anti-Tumor Activation and Maturation of Human Monocyte-Derived DC.International journal of molecular sciences · 2021Article
- Putting on the Brakes: Regulatory Kinases and Phosphatases Maintaining B Cell Anergy.Frontiers in immunology · 2018Review
- Unperturbed Immune Function despite Mutation of C-Terminal Tyrosines in Syk Previously Implicated in Signaling and Activity Regulation.Molecular and cellular biology · 2017Article
- Effective Combination Therapies for B-cell Lymphoma Predicted by a Virtual Disease Model.Cancer research · 2017Article
- Phosphorylation impact on Spleen Tyrosine kinase conformation by Surface Enhanced Raman Spectroscopy.Scientific reports · 2017Article
- RET Functions as a Dual-Specificity Kinase that Requires Allosteric Inputs from Juxtamembrane Elements.Cell reports · 2016Article
- Reconstituted B cell receptor signaling reveals carbohydrate-dependent mode of activation.Scientific reports · 2016Article
- In vitro reconstitution of B cell receptor-antigen interactions to evaluate potential vaccine candidates.Nature protocols · 2016Article
- Calling in SYK: SYK's dual role as a tumor promoter and tumor suppressor in cancer.Biochimica et biophysica acta · 2015Review
- A PREVIOUSLY UNKNOWN UNIQUE CHALLENGE FOR INHIBITORS OF SYK ATP-BINDING SITE: ROLE OF SYK AS A CELL CYCLE CHECKPOINT REGULATOR.EBioMedicine · 2014Article
- Getting Syk: spleen tyrosine kinase as a therapeutic target.Trends in pharmacological sciences · 2014Review
- Encephalomyocarditis virus leader is phosphorylated by CK2 and syk as a requirement for subsequent phosphorylation of cellular nucleoporins.Journal of virology · 2014Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Upon B-cell activation, the signaling subunits Ig-α and Ig-β of the B-cell antigen receptor become phosphorylated not only on tyrosines but also on serine residues. Using a specific antibody, we show that serine 197 (S197) in the cytoplasmic tail of Ig-α is phosphorylated upon B-cell antigen receptor activation, and that this modification inhibits the signal output of the B-cell antigen receptor. Surprisingly, we found that the well-known protein tyrosine kinase Syk (spleen tyrosine kinase) phosphorylates S197 on Ig-α, thus not only activating but also inhibiting signaling from the B-cell antigen receptor. This finding identifies Syk as a dual-specificity kinase and establishes a previously unexplored paradigm for the self-regulation of biological signaling processes.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.