FEBS Letters | |
Phosphorylation and activation of Ca2+/calmodulin‐dependent protein kinase phosphatase by Ca2+/calmodulin‐dependent protein kinase II | |
Fujisawa, Hitoshi1  Kameshita, Isamu1  Ishida, Atsuhiko1  | |
[1] Department of Biochemistry, Asahikawa Medical College, Asahikawa 078-8510, Japan | |
关键词: Calmodulin-dependent protein kinase II; Enzyme activation; Protein phosphatase; Protein phosphorylation; Polylysine; CaMK; Ca2+/calmodulin-dependent protein kinase; 30 kDa CaMKII; 30 kDa fragment of Ca2+/calmodulin-dependent protein kinase II; CaMKPase; Ca2+/calmodulin-dependent protein kinase phosphatase; poly(Lys); poly-l-lysine; poly(Lys)9.6K; poly(Lys)23K and poly(Lys)87K; poly-l-lysine with average molecular weights of 9600; 23 000 and 87 000; respectively; (Lys)5; (Lys)10 and (Lys)20; oligopeptides composed of 5; 10 and 20 lysines; respectively; | |
DOI : 10.1016/S0014-5793(99)00958-8 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
Ca2+/calmodulin-dependent protein kinase phosphatase (CaMKPase) is a protein phosphatase which dephosphorylates autophosphorylated Ca2+/calmodulin-dependent protein kinase II (CaMKII) and deactivates the enzyme (Ishida, A., Kameshita, I. and Fujisawa, H. (1998) J. Biol. Chem. 273, 1904–1910). In this study, a phosphorylation-dephosphorylation relationship between CaMKII and CaMKPase was examined. CaMKPase was not significantly phosphorylated by CaMKII under the standard phosphorylation conditions but was phosphorylated in the presence of poly-l-lysine, which is a potent activator of CaMKPase. The maximal extent of the phosphorylation was about 1 mol of phosphate per mol of the enzyme and the phosphorylation resulted in an about 2-fold increase in the enzyme activity. Thus, the activity of CaMKPase appears to be regulated through phosphorylation by its target enzyme, CaMKII.
【 授权许可】
Unknown
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