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J Biol Chem, Vol. 273, Issue 26, 15980-15984, June 26, 1998

Regulation of Casein Kinase I epsilon  and Casein Kinase I delta  by an in Vivo Futile Phosphorylation Cycle

Ann RiversDagger , Kimberly Fish GietzenDagger , Erica VielhaberDagger , and David M. VirshupDagger §

From the Dagger  Division of Molecular Biology and Genetics, Department of Oncological Sciences, Huntsman Cancer Institute, the § Division of Hematology/Oncology, Department of Pediatrics, and the  Program in Human Molecular Biology and Genetics, University of Utah, Salt Lake City, Utah 84132

Casein kinase I delta  (CKIdelta ) and casein kinase I epsilon  (CKIepsilon ) have been implicated in the response to DNA damage, but the understanding of how these kinases are regulated remains incomplete. In vitro, these kinases rapidly autophosphorylate, predominantly on their carboxyl-terminal extensions, and this autophosphorylation markedly inhibits kinase activity (Cegielska, A., Gietzen, K. F., Rivers, A., and Virshup, D. M. (1998) J. Biol. Chem. 273, 1357-1364). However, we now report that while these kinases are able to autophosphorylate in vivo, they are actively maintained in the dephosphorylated, active state by cellular protein phosphatases. Treatment of cells with the cell-permeable serine/threonine phosphatase inhibitors okadaic acid or calyculin A leads to rapid increases in kinase intramolecular autophosphorylation. Since CKI autophosphorylation decreases kinase activity, this dynamic autophosphorylation/dephosphorylation cycle provides a mechanism for kinase regulation in vivo.

Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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