The inhibitory effect of actin on protein phosphorylation by three dis
tinct protein kinases (CK-II, A-kinase and MAP-kinase) was examined in
vitro. It was found that: (i) actin inhibits the activities of alpha-
monomeric CK-II (CK-II alpha) as well as oligomeric CK-II (alpha(2) be
ta(2)) in a dose-dependent manner, but has no effect on the activities
of the two other kinases; and (ii) actin-induced inhibition of CK-II
activity is due to the binding of actin to the alpha-subunit of CK-II
and is non-competitive with its phosphate accepters. In addition, it i
s demonstrated that actin binds directly to CK-II: both actin and CK-I
I are coprecipitated by anti-serum against Drosophila CK-II beta or by
specific IgG against Ascaris suum muscle actin. The results presented
here suggest that actin can suppress CK-II-mediated signal transducti
on.