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High-Affinity Chimeric Human Granulocyte-Macrophage Colony-Stimulating Factor-Receptor Carrying the Cytoplasmic Domain of the β Subunit But Not the α Subunit Transduces Growth-Promoting Signals in Ba/F3 Cells

Authors
Journal
Biochemical and Biophysical Research Communications
0006-291X
Publisher
Elsevier
Publication Date
Volume
208
Issue
1
Identifiers
DOI: 10.1006/bbrc.1995.1347
Disciplines
  • Design

Abstract

Abstract Granulocyte-macrophage colony-stimulating factor receptor (GMR) is composed of two distinct subunits α and β, and the cytoplasmic domains of both subunits are essential to transduce signals. We further analyzed the role of the cytoplasmic domain of each subunit by constructing chimeric subunits, designated α/β and β/α, by exchanging cytoplasmic domains of the α and β subunits of hGMR. Reconstituted high-affinity chimeric hGMRs, hGMR(α/β,β/α) and hGMR(α/β,β), as well as the wild type hGMR(α,β),transduced signals in Ba/F3 cells. These observations indicate that the original configuration between the extracellular and the cytoplasmic domains of the hGMR(α,β) subunits is not obligatory, and that hGMR(α/β, β) transduced signals through the cytoplasmic domain of the β subunit in an oligomeric form, without involvement of the cytoplasmic domain of the α subunit.

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