Multivalent binding proteins, such as the yeast scaffold protein Steri
le-5, coordinate the location of kinases by serving as platforms for t
he assembly of signaling units. Similarly, in mammalian cells the cycl
ic adenosine 3',5'-monophosphate-dependent protein kinase (PKA) and ph
osphatase 2B [calcineurin (CaN)] are complexed by an A kinase anchorin
g protein, AKAP79. Deletion analysis and binding studies demonstrate t
hat a third enzyme, protein kinase C (PKC), binds AKAP79 at a site dis
tinct from those bound by PKA or CaN. The subcellular distributions of
PKC and AKAP79 were similar in neurons. Thus, AKAP79 appears to funct
ion as a scaffold protein for three multifunctional enzymes.