TY - JOUR
T1 - Dephosphorylation of autophosphorylated Ca2+/calmodulin-dependent protein kinase II by protein phosphatase 2C
AU - Fukunaga, K.
AU - Kobayashi, T.
AU - Tamura, S.
AU - Miyamoto, E.
PY - 1993
Y1 - 1993
N2 - 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.
AB - 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.
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M3 - Article
C2 - 8380154
AN - SCOPUS:0027339550
SN - 0021-9258
VL - 268
SP - 133
EP - 137
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 1
ER -