Traditionally IgA has been regarded as a non-inflammatory antibody, which inhibits adhesion of micro-organisms to the mucosal wall without initiation of inflammatory responses. Recently, however, a dichotomy has been suggested between the actions of secretory IgA (SIgA), which is present at mucosal sites, and serum IgA. SIgA exerts its function as first line of defence by limiting invasion of pathogens. Serum IgA in turn may be engaged in inflammatory responses after breaching of mucosal wall integrity. Several receptors for IgA have been described. However, the-as yet-best characterized prototypic Fc receptor for IgA, FcalphaRI (CD89), is the most likely candidate for initiation of inflammatory responses, as it binds poorly to SIgA, but vigorously triggers potent effector functions upon binding to serum IgA. Here, new insights in IgA-FcalphaRI binding are described and the functional implications of these interactions are discussed.