ArticleProceedings of the National Academy of Sciences of the United States of America1999
Molecular cloning of a docking protein, BRDG1, that acts downstream of the Tec tyrosine kinase.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 62 citations in OpenAlex.
- Imperative role of adaptor proteins in macrophage toll-like receptor signaling pathways.Future science OA · 2024Review
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- Signal-transducing adaptor protein 1 (STAP1) in microglia promotes the malignant progression of glioma.Journal of neuro-oncology · 2023Article
- The Functional Properties and Physiological Roles of Signal-Transducing Adaptor Protein-2 in the Pathogenesis of Inflammatory and Immune Disorders.Biomedicines · 2022Review
- Reticular Basement Membrane Thickness Is Associated with Growth- and Fibrosis-Promoting Airway Transcriptome Profile-Study in Asthma Patients.International journal of molecular sciences · 2021Article
- COPD patients with chronic bronchitis and higher sputum eosinophil counts show increased type-2 and PDE4 gene expression in sputum.Journal of cellular and molecular medicine · 2021Article
- Signal-transducing adapter protein-1 is required for maintenance of leukemic stem cells in CML.Oncogene · 2020Article
- Taking One Step Back in Familial Hypercholesterolemia:Arteriosclerosis, thrombosis, and vascular biology · 2020Article
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- Genes Potentially Associated with Familial Hypercholesterolemia.Biomolecules · 2019Review
- Evaluation of the role of STAP1 in Familial Hypercholesterolemia.Scientific reports · 2019Article
- High STAP1 expression in DUX4-rearranged cases is not suitable as therapeutic target in pediatric B-cell precursor acute lymphoblastic leukemia.Scientific reports · 2018Article
- Small Molecule Inhibitors Targeting Tec Kinase Block Unconventional Secretion of Fibroblast Growth Factor 2.The Journal of biological chemistry · 2016Article
- Interferon-beta therapy in multiple sclerosis: the short-term and long-term effects on the patients' individual gene expression in peripheral blood.Molecular neurobiology · 2013Article
- Extensive gene-specific translational reprogramming in a model of B cell differentiation and Abl-dependent transformation.PloS one · 2012Article
- Loops govern SH2 domain specificity by controlling access to binding pockets.Science signaling · 2010Article
- Prediction of phosphotyrosine signaling networks using a scoring matrix-assisted ligand identification approach.Nucleic acids research · 2008Article
- Mimicry of a constitutively active pre-B cell receptor in acute lymphoblastic leukemia cells.The Journal of experimental medicine · 2005Article
- Signaling network of the Btk family kinases.Oncogene · 2000Article
- A novel adaptor-like protein which is a substrate for the non-receptor tyrosine kinase, BRK.Oncogene · 2000Article
Corrections and comments
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Authors and funding
11 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tec, Btk, Itk, Bmx, and Txk constitute the Tec family of protein tyrosine kinases (PTKs), a family with the distinct feature of containing a pleckstrin homology (PH) domain. Tec acts in signaling pathways triggered by the B cell antigen receptor (BCR), cytokine receptors, integrins, and receptor-type PTKs. Although upstream regulators of Tec family kinases are relatively well characterized, little is known of the downstream effectors of these enzymes. The yeast two-hybrid system has identified several proteins that interact with the kinase domain of Tec, one of which is now revealed to be a previously unknown docking protein termed BRDG1 (BCR downstream signaling 1). BRDG1 contains a proline-rich motif, a PH domain, and multiple tyrosine residues that are potential target sites for Src homology 2 domains. In 293 cells expressing recombinant BRDG1 and various PTKs, Tec and Pyk2, but not Btk, Bmx, Lyn, Syk, or c-Abl, induced marked phosphorylation of BRDG1 on tyrosine residues. BRDG1 was also phosphorylated by Tec directly in vitro. Efficient phosphorylation of BRDG1 by Tec required the PH and SH2 domains as well as the kinase domain of the latter. Furthermore, BRDG1 was shown to participate in a positive feedback loop by increasing the activity of Tec. BRDG1 transcripts are abundant in the human B cell line Ramos, and the endogenous protein underwent tyrosine phosphorylation in response to BCR stimulation. BRDG1 thus appears to function as a docking protein acting downstream of Tec in BCR signaling.
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