Induction of the antigen receptor expression on B lymphocytes results in rapid competence for signaling of SLP-65 and Syk
| Autor: | Michael Reth, Jürgen Wienands, Yong Zhang, Christa Zürn |
|---|---|
| Rok vydání: | 1998 |
| Předmět: |
Cell signaling
B-cell receptor Molecular Sequence Data Cre recombinase Syk Receptors Antigen B-Cell Biology Transfection General Biochemistry Genetics and Molecular Biology Cell Line Viral Proteins LYN hemic and lymphatic diseases Syk Kinase Amino Acid Sequence Phosphorylation Molecular Biology Adaptor Proteins Signal Transducing Recombination Genetic B-Lymphocytes Enzyme Precursors Expression vector General Immunology and Microbiology Base Sequence Integrases General Neuroscience breakpoint cluster region Intracellular Signaling Peptides and Proteins Biological Transport Protein-Tyrosine Kinases Phosphoproteins Molecular biology Tamoxifen src-Family Kinases Gene Expression Regulation Tyrosine Vanadates Carrier Proteins Signal Transduction Research Article |
| Zdroj: | The EMBO journal. 17(24) |
| ISSN: | 0261-4189 |
| Popis: | The binding of antigen to the B cell antigen receptor (BCR) results in the activation of protein tyrosine kinases (PTKs) such as Lyn and Syk, and the phosphorylation of several substrate proteins including HS1 and SLP-65. How these signaling elements are connected to the BCR is not well understood. Using an expression vector for a tamoxifen-regulated Cre recombinase, we have developed a method that allows the inducible expression of the BCR. Disruption of the VH leader reading frame of the immunoglobulin heavy chain by two loxP sites is overcome by Cre-mediated DNA recombination and results in the cell surface expression of the BCR starting 4 h after exposure of transfected B cells to tamoxifen. This method can, in principle, be employed for the inducible expression of any secreted or type I transmembrane protein. By monitoring the activation of signaling elements in pervanadate-stimulated B cells expressing different levels of the BCR, we show here that phosphorylation of SLP-65 and Syk, but not of Lyn, is strictly dependent on the expression of the BCR on the cell surface. These data suggest that the BCR reorganizes its signaling molecules as soon as it appears on the cell surface. |
| Databáze: | OpenAIRE |
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