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J. Biol. Chem., Vol. 261, Issue 21, 9614-9621, Jul, 1986
D Bar-Zvi and D Branton
Incubation of clathrin-coated vesicles with Mg2+-[gamma-32P]ATP results in
the autophosphorylation of a 50-kDa polypeptide (pp50) (Pauloin, A.,
Bernier, I., and Jolles, P. (1982) Nature 298, 574-576). We describe here a
second protein kinase that is associated with calf brain and liver coated
vesicles. This kinase, which phosphorylates casein and phosvitin but not
histone and protamine using either ATP or GTP, co- fractionates with coated
vesicles as assayed by gel filtration, electrophoresis, and sedimentation.
The enzyme can be extracted with 0.5 M Tris-HCl or 1 M NaCl, and can be
separated from the pp50 kinase as well as the other major coat proteins. We
identified this enzyme as casein kinase II based on physical and catalytic
properties and by comparative studies with casein kinase II isolated from
brain cytosol. It has a Stokes radius of 4.5 nm, a catalytic moiety of
approximately 45 kDa, and labels a polypeptide of 26 kDa when the pure
enzyme is assayed for autophosphorylation. Its activity is inhibited by
heparin and not affected by cAMP, phospholipids, or calmodulin. This
protein kinase preferentially phosphorylates clathrin beta-light chain. The
phosphorylation is markedly stimulated by polylysine and inhibited by
heparin. Isolated beta-light chain as well as beta-light chain in
triskelions or in intact coated vesicles is phosphorylated. All of the
phosphate (0.86 mol of Pi/mol of clathrin beta-light chain) is incorporated
into phosphoserine.
Clathrin-coated vesicles contain two protein kinase activities. Phosphorylation of clathrin beta-light chain by casein kinase II
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