[HTML][HTML] Role of COOH-terminal Phosphorylation in the Regulation of Casein Kinase Iδ (∗)
PR Graves, PJ Roach - Journal of Biological Chemistry, 1995 - ASBMB
Casein kinase Iδ is a member of the casein kinase I (CKI) family, a group of second
messenger independent protein kinases. We present evidence that the COOH-terminal
domain of CKIδ has regulatory properties. CKIδ expressed in Escherichia coli was activated
by heparin, as found previously, and by treatment with the catalytic subunit of type-1 protein
phosphatase (CS1). Concomitant with activation by CS1, there was a reduction in the
apparent molecular weight of CKIδ from 55,000 to 49,000 as judged by polyacrylamide gel …
messenger independent protein kinases. We present evidence that the COOH-terminal
domain of CKIδ has regulatory properties. CKIδ expressed in Escherichia coli was activated
by heparin, as found previously, and by treatment with the catalytic subunit of type-1 protein
phosphatase (CS1). Concomitant with activation by CS1, there was a reduction in the
apparent molecular weight of CKIδ from 55,000 to 49,000 as judged by polyacrylamide gel …
