Reconstitution of a Mg-ATP-dependent protein phosphatase and its activation through a phosphorylation mechanism |
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Authors: | Brian A Hemmings Therese J Resink Philip Cohen |
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Institution: | A.N. Belozersky Laboratory of Molecular Biology and Bioorganic Chemistry, Moscow State University, Moscow 117234, USSR |
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Abstract: | A Mg-ATP-dependent protein phosphatase has been reconstituted from the catalytic subunit of protein phosphatase-1 and inhibitor-2, and consists of a 1:1 complex between these proteins. Activation of this enzyme by glycogen synthase kinase-3 and Mg-ATP results from the phosphorylation of inhibitor-2 on a threonine residue(s) and is accompanied by the dissociation of the complex. The results prove that protein phosphatase-1 and the Mg-ATP-dependent protein phosphatase contain the same catalytic subunit, and that they are interconvertible forms of the same enzyme. |
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Keywords: | Protein phosphatase-1 Glycogen synthase kinase Inhibitor-2 Phosphorylase Thiophosphorylation |
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