Regulation of FcεRI-mediated signaling by an adaptor protein STAP-2/BSK in rat basophilic leukemia RBL-2H3 cells
| Autor: | Takashi Yamamoto, Akihiko Yoshimura, Noriko Sato, Tadashi Matsuda, Mayu Minoguchi, Taro Yumioka, Yuichi Sekine |
|---|---|
| Rok vydání: | 2003 |
| Předmět: |
Recombinant Fusion Proteins
Biophysics Syk Protein tyrosine phosphatase Biology Biochemistry Receptor tyrosine kinase chemistry.chemical_compound Genes Reporter Tumor Cells Cultured Animals Humans Syk Kinase Mast Cells Molecular Biology Adaptor Proteins Signal Transducing Enzyme Precursors NFATC Transcription Factors Phospholipase C gamma Receptors IgE Kinase Intracellular Signaling Peptides and Proteins Degranulation Nuclear Proteins Signal transducing adaptor protein Tyrosine phosphorylation Cell Biology Protein-Tyrosine Kinases Phosphoproteins Rats Cell biology DNA-Binding Proteins Adaptor Proteins Vesicular Transport Leukemia Basophilic Acute chemistry Type C Phospholipases biology.protein Calcium Tyrosine kinase Signal Transduction Transcription Factors |
| Zdroj: | Biochemical and Biophysical Research Communications. 306:767-773 |
| ISSN: | 0006-291X |
| DOI: | 10.1016/s0006-291x(03)01042-8 |
| Popis: | Crosslinking of multivalent antigen bound IgE transduces FcepsilonRI mediated signaling cascades, which activate nonreceptor-type protein-tyrosine kinases and subsequent tyrosine phosphorylation of cellular proteins, and these are critical elements for degranulation in mast cells. We cloned a novel adaptor molecule, signal transducing adaptor protein (STAP)-2 containing PH and SH2-like domains as a c-fms interacting protein. STAP-2 was identical to a recently cloned adaptor molecule, BKS, a substrate of BRK (breast tumor kinase) tyrosine kinase, although its function is still unknown. To examine a novel function of STAP-2/BSK, we expressed STAP-2/BSK or its mutants in rat basophilic leukemia RBL-2H3 cells. Overexpression of STAP-2/BSK resulted in a suppression of FcepsilonRI-mediated calcium mobilization and degranulation. FcepsilonRI-induced tyrosine phosphorylation of phospholipase C-gamma (PLC-gamma) but not Syk was significantly suppressed in these cells. Furthermore, STAP-2/BSK associated with PLC-gamma in vivo. These data indicate that STAP-2/BSK negatively controls the FcepsilonRI-mediated calcium mobilization and degranulation by direct modulation of tyrosine phosphorylation of PLC-gamma. |
| Databáze: | OpenAIRE |
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