Fyn binds to and phosphorylates T cell immunoglobulin and mucin domain-1 (Tim-1)
| Autor: | Elizabeth Stepniak, Paul B. Rothman, Judit Knisz, John D. Colgan, Melody Singh, Paul D. Rennert, Geri L. Traver, Miranda L. Curtiss, Natalie Manhica, Bruce S. Hostager |
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| Rok vydání: | 2011 |
| Předmět: |
T-Lymphocytes
Immunology Proto-Oncogene Proteins c-fyn environment and public health Article Receptor tyrosine kinase Cell Line Mice FYN Animals Humans Hepatitis A Virus Cellular Receptor 1 Phosphorylation RNA Small Interfering Tyrosine Molecular Biology B-Lymphocytes Mice Inbred BALB C Membrane Glycoproteins Tyrosine-protein kinase CSK biology Epithelial Cells Molecular biology enzymes and coenzymes (carbohydrates) Tyrosine kinase 2 biology.protein Receptors Virus Tyrosine kinase Signal Transduction Proto-oncogene tyrosine-protein kinase Src |
| Zdroj: | Molecular Immunology. 48:1424-1431 |
| ISSN: | 0161-5890 |
| DOI: | 10.1016/j.molimm.2011.03.023 |
| Popis: | The gene encoding T cell immunoglobulin and mucin domain-1 (TIM-1) is linked to atopy and asthma susceptibility in mice and humans. TIM-1 is a transmembrane protein expressed on activated lymphocytes and appears to have a role as a co-stimulatory receptor in T cells. The protein has not been shown to have enzymatic activity but contains a site within its cytoplasmic tail predicted to be a target for tyrosine kinases. Here, we show that Tim-1 can associate with the kinase Fyn, a member of the Src family of tyrosine kinases. This association does not require Fyn’s kinase activity and is independent of the phosphorylation of a conserved tyrosine present within the cytoplasmic tail of Tim-1. Fyn is necessary for phosphorylation of this tyrosine in Tim-1 and the phosphorylation of Tim-1 varies with the levels of Fyn present in cells. These data suggest a role for Fyn in the signaling downstream of Tim-1. |
| Databáze: | OpenAIRE |
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