Following the initial identification of protein kinase C (PKC) by Nish
izuka and co-workers in the late seventies, a wealth of information on
this protein kinase has accumulated. Perhaps most striking was the re
alization that PKC is not just a single polypeptide but in fact consis
ts of a large family of related proteins. These PKC isotypes are uniqu
e, not only with respect to primary structure, but also on the basis o
f expression patterns, subcellular localization, activation in vitro a
nd responsiveness to extracellular 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 i
n the cell.