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Differential recruitment of accessory molecules by FcγRI during monocyte differentiation

Aggregation of the human high‐affinity receptor for immunoglobulin G, FcγRI, results in initiation of intracellular signaling cascades. However, as the receptor contains no known signalingmotif, it is required to recruit an accessory molecule. The γ chain has been proposed to fulfil this role. Here, we show that in U937 cells differentiated to a more macrophage‐like phenotype with dibutyryl cAMP, FcγRI no longer signals through the γ chain but rather uses FcγRIIa to initiate tyrosine phosphorylation. Expression of the γ chain is, however, increased in the dbcAMP‐induced cells, but here the γ chain specifically associates with the IgA receptor, FcαRI. Recruitment of the γ chain either by FcγRI in cytokine‐primed cells or by FcαRI indbcAMP‐induced cells couples ligand binding to the activation of phosphatidyl choline‐specific phospholipase D.