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Swapping between Fas and granulocyte colony-stimulating factor receptor

T Takahashi1, M Tanaka, J Ogasawara

  • 1Osaka Bioscience Institute, 6-2-4 Furuedai, Suita, Japan.

The Journal of Biological Chemistry
|July 19, 1996
PubMed
Summary
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Researchers created hybrid receptors by combining Fas and granulocyte colony-stimulating factor receptor (G-CSFR). This study shows that different receptor families can exchange functions, impacting cell signaling pathways.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Immunology

Background:

  • Fas receptor initiates apoptosis upon Fas ligand binding.
  • Granulocyte colony-stimulating factor receptor (G-CSFR) regulates neutrophil development.
  • Receptor families typically mediate distinct cellular functions.

Purpose of the Study:

  • To investigate functional exchange between the Fas and G-CSFR signaling pathways.
  • To construct and express chimeric receptors combining Fas and G-CSFR domains.
  • To determine how domain swapping affects receptor-mediated cell signaling.

Main Methods:

  • Construction of Fas/G-CSFR hybrid receptors.
  • Expression of chimeric receptors in mouse T cell (WR19L) and myeloid (FDC-P1) lines.

Related Experiment Videos

  • Stimulation of cells with Fas ligand, anti-Fas antibody, G-CSF, and anti-G-CSFR antibody.

    • Main Results:

    • Chimeric receptors with Fas extracellular and G-CSFR cytoplasmic regions induced proliferation upon Fas stimulation.
    • Chimeric receptors with G-CSFR extracellular and Fas cytoplasmic regions did not induce apoptosis with G-CSF but were killed by anti-G-CSFR antibody.
    • Demonstrated functional interchangeability between different receptor families.

    Conclusions:

    • Receptors from distinct families can functionally substitute for each other.
    • G-CSFR homodimerization transduces growth signals.
    • Fas receptor requires oligomerization (likely trimerization) for apoptotic signal transduction.