| First Author | Takahashi T | Year | 1996 |
| Journal | J Biol Chem | Volume | 271 |
| Issue | 29 | Pages | 17555-60 |
| PubMed ID | 8663376 | Mgi Jnum | J:34155 |
| Mgi Id | MGI:81624 | Doi | 10.1074/jbc.271.29.17555 |
| Citation | Takahashi T, et al. (1996) Swapping between Fas and granulocyte colony-stimulating factor receptor. J Biol Chem 271(29):17555-60 |
| abstractText | Fas belongs to the tumor necrosis factor/nerve growth factor receptor family. The Fas ligand binds to its receptor, Fas, and induces apoptosis in Fas-bearing cells. The granulocyte colony-stimulating factor receptor (G-CSFR) is a member of the hemopoietic growth factor receptor family. G-CSF induces its dimerization and regulates the proliferation and differentiation of neutrophilic granulocytes. We constructed hybrid receptors between Fas and G-CSFR and expressed them in the mouse T cell line WR19L or the mouse myeloid interleukin-3-dependent FDC-P1 cell line. The Fas ligand or an agonistic anti-Fas antibody stimulated proliferation of the FDC-P1 transformants expressing a chimera consisting of the Fas extracellular and G-CSFR cytoplasmic regions. On the other hand, G-CSF could not induce apoptosis in the transformants expressing the chimera consisting of the G-CSFR extracellular and Fas cytoplasmic regions, but these cells were killed by a polyclonal antibody against G-CSFR. These results indicated that receptors belonging to different receptor families can be functionally exchanged and confirm that a homodimer of G-CSFR can transduce the growth signal, whereas Fas must be oligomerized (probably trimerized) to transduce the apoptotic signal. |
