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.
Original language | English |
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Pages (from-to) | 319-324 |
Number of pages | 6 |
Journal | FEBS Letters |
Volume | 150 |
Issue number | 2 |
DOIs | |
Publication status | Published - 27 Dec 1982 |
Keywords
- Glycogen synthase kinase
- Inhibitor-2
- Phosphorylase
- Protein phosphatase-1
- Thiophosphorylation
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology