Compartmentalized protein phosphorylation/dephosphorylation in glycogen particles from rabbit skeletal muscle.
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.
Gruppuso
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PA
Section of Biochemistry, Brown University, Providence, RI 02912.
Brautigan
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DL
D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D002118:Calcium / Q000502:physiology; D005260:Female; D006003:Glycogen / Q000378:metabolism*; D008274:Magnesium / Q000502:physiology; D009124:Muscle Proteins / Q000378:metabolism*; D009132:Muscles / Q000378:metabolism*; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism; D010764:Phosphorylase Kinase / Q000378:metabolism; D010766:Phosphorylation; D011817:Rabbits
D009124:Muscle Proteins; D000255:Adenosine Triphosphate; D006003:Glycogen; D010764:Phosphorylase Kinase; D010744:Phosphoric Monoester Hydrolases; D008274:Magnesium; D002118:Calcium