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Phosphorylation of protein phosphatase inhibitor-1 by protein kinase C

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By Bogachan Sahin, Hongjun Shu, Joseph Fernandez, Ali El-Armouche
| tu-dresden.de
Inhibitor-1 becomes a potent inhibitor of protein phosphatase 1 when phosphorylated by cAMP-dependent protein kinase at Thr35. Moreover, Ser67 of inhibitor-1 serves as a substrate for cyclin-dependent kinase 5 in the brain. Here, we report that dephosphoinhibitor-1 but not phospho-Ser67 inhibitor-1 was efficiently phosphorylated by protein kinase C at Ser65 in vitro. In contrast, Ser67 phosphorylation by cyclin-dependent kinase 5 was unaffected by phospho-Ser 65.
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