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Vol. 273, Issue 3, 1357-1364, January 16, 1998

Autoinhibition of Casein Kinase I  (CKI) Is Relieved by Protein Phosphatases and Limited Proteolysis

Aleksandra Cegielska, Kimberly Fish Gietzen, Ann Rivers, and David M. Virshup^¶

From the  Division of Molecular Biology and Genetics, Department of Oncological Sciences, Huntsman Cancer Institute, ^¶ Division of Hematology/Oncology, Department of Pediatrics, and the  Program in Human Molecular Biology and Genetics, University of Utah, Salt Lake City, Utah 84112

Casein kinase I  (CKI) is a member of the CKI gene family, members of which are involved in the control of SV40 DNA replication, DNA repair, and cell metabolism. The mechanisms that regulate CKI activity and substrate specificity are not well understood. We report that CKI, which contains a highly phosphorylated 123-amino acid carboxyl-terminal extension not present in CKI, is substantially less active than CKI in phosphorylating a number of substrates including SV40 large T antigen and is unable to inhibit the initiation of SV40 DNA replication. Two mechanisms for the activation of CKI have been identified. First, limited tryptic digestion of CKI produces a protease-resistant amino-terminal 39-kDa core kinase with several-fold enhanced activity. Second, phosphatase treatment of CKI activates CKI 5-20-fold toward T antigen. Similar treatment of a truncated form of CKI produced only a 2-fold activation. Notably, this activation was transient; reautophosphorylation led to a rapid down-regulation of the kinase within 5 min. Phosphatase treatment also activated CKI toward the novel substrates IB and Ets-1. These mechanisms may serve to regulate CKI and related forms of CKI in the cell, perhaps in response to DNA damage.

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