Distinct signal transduction through the tyrosine-containing domains of the granulocyte colony-stimulating factor receptor

Akikazu Yoshikawa, Hiroshi Murakami, Shigekazu Nagata

Research output: Contribution to journalArticle

70 Citations (Scopus)

Abstract

The receptor for granulocyte colony-stimulating factor (G-CSFR) is a hemopoietic growth factor receptor, which mediates proliferation and differentiation signals. The cytoplasmic region of G-CSFR carries four tyrosine residues in its C-terminal half. We constructed mutant receptors in which each tyrosine residue of G-CSFR was mutated to phenylalanine. Two mutant receptors (Tyr703 and Tyr728) neither transduced the growth-inhibitory signal nor induced the neutrophil-specific myeloperoxidase (MPO) gene. The Tyr703 mutant did not induce morphological changes in cells, whereas transformants expressing the Tyr728 mutant adhered to plates with a macrophage-like morphology upon G-CSF stimulation. Mutation of the most distal tyrosine residue (Tyr763) abolished the ability of G-CSFR to stimulate the tyrosine phosphorylation of a cellular protein with an M(r) of 54 kDa. These results indicated that the regions around the three tyrosine residues of G-CSFR play essential and distinct roles in signal transduction.

Original languageEnglish
Pages (from-to)5288-5296
Number of pages9
JournalEMBO Journal
Volume14
Issue number21
Publication statusPublished - Nov 27 1995
Externally publishedYes

Keywords

  • Colony-stimulating factor
  • G-CSF receptor
  • Neutrophilic differentiation
  • Site-directed mutagenesis
  • Tyrosine phosphorylation

ASJC Scopus subject areas

  • Neuroscience(all)
  • Molecular Biology
  • Biochemistry, Genetics and Molecular Biology(all)
  • Immunology and Microbiology(all)

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