Cell surface receptors for the Fc portion of immunoglobulin confer on most cells of the immune system the ability to communicate with the humoral antibody response. These Fc receptors are known to be particularly important for the function of various effector cells, such as macrophages, since they are involved in mediating a variety of activities including endocytosis, antibody-dependent cellular cytotoxicity, and triggering the release of potent inflammatory agents. Over the past few years, a considerable amount has been learned about the structure and functions of the Fc receptors expressed by murine and human cells, due to the availability of specific anti-receptor antibodies and the isolation of Fc receptor cDNA clones. In general, these receptors are transmembrane proteins whose extracellular domains contain two immunoglobulin-like regions and are thus members of the immunoglobulin gene family. Their domain structure consists of a glycosylated extracellular domain, a single membrane-spanning segment, and a relatively long cytoplasmic domain. The cytoplasmic tails exhibit a surprising degree of variation in length and amino acid sequence. This review summarizes some recent information concerning the structure and expression of the Fc receptors found on murine and human macrophages and lymphocytes. Particular attention is paid to the functional activities of these receptors, and the possible relationship between receptor function and receptor structure.