The subunit of the receptor for human granulocyte-macrophage colony-stimulating factor (GM-CSF) is a glycoprotein containing 11 potential N-glycosylation sites in the extracellular domain. We examined the role of N-glycosylation on subunit membrane localization and function. Tunicamycin, an N-glycosylation inhibitor, markedly inhibited GM-CSF binding, GM-CSF-induced deoxyglucose uptake, and protein tyrosine phosphorylation in HL-60(eos) cells but did not affect cell surface expression of the subunit as detected by an anti- subunit monoclonal antibody. In COS cells expressing the subunit and treated with tunicamycin, N-unglycosylated subunit was expressed and transported to the cell surface but was not capable of binding GM-CSF. High affinity binding in COS cells expressing both and subunits was also blocked by tunicamycin treatment. These studies indicate that N-linked oligosaccharides are essential for subunit ligand binding and signaling by the human GM-CSF receptor.

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