Abstract
To shed light on the paradoxical behaviour of calmodulin, whose phosphorylation is inhibited by the regulatory β-subunit of protein kinase CK2, a series of peptides encompassing the phosphoacceptor sites of calmodulin have been synthesized and assayed as substrates of CK2 α-subunit either alone or combined with the β-subunit. The shortest peptide whose phosphorylation is reduced instead of being enhanced by the β-subunit encompasses the sequence 68-106, including the central helix and the Ca2+-binding loop-III. In contrast, the phosphorylation of a peptide encompassing loop II and the central helix (54-92) is stimulated, like that of several shorter peptides, by the β-subunit. Our data localize to the C-terminal domain of calmodulin the structural elements that are responsible for inverted susceptibility to β-subunit regulation.
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