It has been demonstrated that okadaic acid-insensitive protein phosphatases are involved in dephosphorylation of autophosphorylated Ca2+/calmodulin-dependent protein kinase II (CaM kinase II) in rat cerebellar granule cells (Fukunaga, K., Rich, D. P., and Soderling, T. R. (1989) J. Biol. Chem. 264, 21830-21836). In the present study, recombinant rat protein phosphatase 2C (PrP-2C) expressed in Escherichia coli could dephosphorylate both Thr(286/287) and Thr(305/306) phosphorylation sites of CaM kinase II, which are responsible for the generation of Ca2+- independent activity and the inhibition of the total activity, respectively. The dephosphorylation of Thr(286/287) and Thr(305/306) was accomplished within 15 min at 0 °C and totally dependent on Mg2+. Phosphopeptide mapping of the CNBr-cleaved 32P-labeled CaM kinase II revealed that PrP-2C was relatively specific for dephosphorylation of Thr(286/287) and Thr(305/306) in the autophosphorylated CaM kinase II. These results suggest that PrP-2C has a role in the regulation of the Ca2+-independent activity of CaM kinase II in the neural cells.
|Number of pages||5|
|Journal||Journal of Biological Chemistry|
|Publication status||Published - 1993|
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology