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pubmed:abstractText |
Activation of phosphorylase in intact glycogen particles from skeletal muscle by Ca2+ and MgATP is known as flash activation. By using [gamma-32P]ATP to monitor protein phosphorylation, we have demonstrated that there is, coincident with phosphorylase activation and inactivation, coordinated phosphorylation/dephosphorylation of phosphorylase, glycogen synthase, the beta-subunit of phosphorylase kinase and proteins of Mr = 43,000 and 32,000. Our results show that within the glycogen particle phosphorylase kinase and type-1 protein phosphatase are organized to allow access to a set of protein components. This arrangement may contribute to the reciprocal regulation of their activities.
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