Amino acid sequence and expression of the hepatic glycogen-binding (GL-subunit of protein phosphatase-1

Martin J. Doherty, Greg Moorhead, Nick Morrice, Philip Cohen, Patricia T.W. Cohen

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    140 Citations (Scopus)


    A full-length cDNA encoding the putative hepatic glycogen-binding (GL) subunit of protein phosphatase-1 (PP1) was isolated from a rat liver library. The deduced amino acid sequence (284 residues, 32.6 kDa) was 23% identical (39% similar) to the N-terminal region of the glycogen-binding (GM) subunit of PP1 from striated muscle. The similarities between GM and GL were most striking between residues 63-86, 144-166 and 186-227 of human GM (∼40% identity), nearly all the identities with the putative yeast homologue GAC1 being located between 144-166 and 186-227. The cDNA was expressed in E. coli, and the expressed protein transformed the properties of PP1 to those characteristic of the hepatic glycogen-associated enzyme. These experiments establish that the cloned protein is GL.

    Original languageEnglish
    Pages (from-to)294-298
    Number of pages5
    JournalFEBS Letters
    Issue number3
    Publication statusPublished - 20 Nov 1995


    • Cyclic AMP-dependent protein kinase
    • Glycogen
    • Glycogen metabolism
    • Protein phosphatase
    • Targetting subunit

    ASJC Scopus subject areas

    • Biophysics
    • Structural Biology
    • Biochemistry
    • Molecular Biology
    • Genetics
    • Cell Biology


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