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• W80242518 abstract "Publisher Summary This chapter elaborates regulation of Ca 2+ /calmodulin-dependent protein kinase II by autophosphorylation/dephosphorylation. In many neural tissues and tissues innervated by them, intracellular changes in Ca 2+ concentrations are known to regulate processes underlying cell contractility, cytoskeletal functions and cell–cell communication. In forebrain, CaM-KII is present in cytosolic and particulate cellular compartments. The effects of autophosphorylation on CaM-KII activity toward the subsequent phosphorylation of synapsin I was assessed by a sequential two-stage (I and II) assay. When autophosphorylated CaM-KII was incubated with protein phosphatase type-1 (PrP-1) for 20 minutes at 30°C, 80% and 85% of the 32 P associated with the 50 and 60 kDa subunits of CaM-KII were removed, respectively. It was indicated that the in vitro autophosphorylation of CaM-KII produces an enzyme whose properties are quite different from that of the unphosphorylated kinase. Ca 2+ /CaM-dependent form of cytosolic CaM-KII can be regenerated from the autophosphorylated kinase by dephosphorylation with purified type-1 protein phosphatase. Recent experiments indicate that the phosphorylation of CaM-KII does occur in brain tissue slices differences between in situ vs. in vitro phosphorylation properties have been observed." @default.
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• W80242518 date "1987-01-01" @default.
• W80242518 modified "2023-10-16" @default.
• W80242518 title "Regulation of Ca2+/Calmodulin-Dependent Protein Kinase II By Autophosphorylation/Dephosphorylation" @default.
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• W80242518 doi "https://doi.org/10.1016/b978-0-12-521040-9.50035-8" @default.
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