Following the initial identification of protein kinase C (PKC) by Nishizuka and co-workers in the late seventies, a wealth of information on this protein kinase has accumulated. Perhaps most striking was the realization that PKC is not just a single polypeptide but in fact consists of a large family of related proteins. These PKC isotypes are unique, not only with respect to primary structure, but also on the basis of expression patterns, subcellular localization, activation in vitro and responsiveness to extra-cellular signals. This review focuses on the heterogeneity within the PKC family and highlights some of the recent evidence that the isotypes might have separate and unique functions in the cell.