Phosphorylation of the phosphatase modulator subunit (inhibitor‐2) by casein kinase‐1 Identification of the phosphorylation sites
Open Access
- 29 June 1992
- journal article
- Published by Wiley in FEBS Letters
- Vol. 305 (2) , 121-124
- https://doi.org/10.1016/0014-5793(92)80877-j
Abstract
The isolated modulator subunit of the inactive protein phosphatase‐1 is phosphorylated in vitro by casein kinase‐1 at two different site Ser‐86 and Ser‐174. The Ser‐86 site is a common target for casein kinase‐1 and casein kinase‐2, but is preferentially phosphorylated by the former enzyme. The Ser‐174 site seems to be specific for casein kinase‐1, and is phosphorylated at a slower rate. These results give a new insight into the in vitro phosphorylation pattern of the modulator subunit of the phosphatase and provides additional data on the specificity of casein kinase‐1.Keywords
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