Phosphorylation of τ Protein by Casein Kinase‐1 Converts It to an Abnormal Alzheimer‐Like State

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Abstract
The microtubule‐associated protein τ is abnormally hyperphosphorylated in Alzheimer's disease. Both proline‐dependent protein kinases (PDPKs) and non‐PDPKs are involved in this hyperphosphorylation of τ. Several PDPKs can phosphorylate τ in vitro and induce Alzheimer‐like epitopes to many phosphorylation‐dependent antibodies. A similar induction has not been reported with non‐PDPKs. In this study we have evaluated six non‐PDPKs [cyclic AMP‐dependent (A‐kinase), calcium/phospholipid‐dependent (C‐kinase), casein kinase‐1 (CK‐1), casein kinase‐2 (CK‐2), calcium/calmodulin‐dependent protein kinase II, and calcium/calmodulin‐dependent protein kinase from rat cerebellum] for their abilities to induce Alzheimer‐like epitopes on τ. Such epitopes were induced by A‐kinase, C‐kinase, CK‐1, and CK‐2, but the degree of induction achieved by CK‐1 was much greater than with the other kinases. These results suggest that CK‐1 may play an important role in the conversion of τ from the normal to the abnormal phosphorylation state in Alzheimer's disease.

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