Cyclic GMP is recognized as an important intracellular mediator of extracellular signals such as nitric oxide and natriuretic peptides. Cyclic GMP interacts with three types of intracellular receptor proteins: cGMP-dependent protein kinases, cGMP-regulated ion channels, and cGMP-regulated cyclic nucleotide phosphodiesterases. This means that cGMP can alter cell function through protein phosphorylation or through mechanisms not directly related to protein phosphorylation. Cyclic GMP appears to regulate a number of intracellular processes, such as vascular smooth muscle relaxation and neutrophil activation, through these receptor proteins in the cell. It is also becoming clear that the localization of these cGMP receptor proteins in the cell is an important factor in the regulation of cell function by cGMP.