Human epidermal Langerhans cells (LC) express variable amounts of the high affinity receptor for IgE (FcεRI); the strongest expression is characteristic of atopic dermatitis. The receptor is suggested to take part in the pathophysiology of this disease by acting as a link between aeroallergens and Ag-specific T cells in an IgE-mediated, delayed-type hypersensitivity reaction. In the present study we show that even in the absence of surface expression, normal LC maintain an intracellular pool of the α-chain of FcεRI (FcεRIα) of the same mw as the surface-bound FcεRIα that is able to bind significant amounts of IgE. The lack of surface expression is linked to the absence or very low expression of the γ-chain (FcεRIγ). Moreover, the amount of FcεRIα expressed at the cell surface significantly correlates with the amount of FcεRIγ. LC differentiation toward lymphoid dendritic cells is accompanied by the disappearance of transcripts for FcεRIα, but not for FcεRIγ. This leads to a rapid decrease in the intracellular and surface levels of FcεRIα, which cannot be influenced by IL-4, IgE, or other agents. Overall, our findings suggest that these mechanisms enable LC to be highly versatile APCs by rapidly adapting the surface level of FcεRI to distinct inflammatory environments.