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Biochem J. 1998 Dec 15;336 ( Pt 3):699-704.

Identification of the separate domains in the hepatic glycogen-targeting subunit of protein phosphatase 1 that interact with phosphorylase a, glycogen and protein phosphatase 1.

Author information

1
Medical Research Council Protein Phosphorylation Unit, Department of Biochemistry, University of Dundee, Dundee DD15EH, Scotland, U.K. cgarmstrong@bad.dundee.ac.uk

Abstract

Deletion and mutational analyses of the rat liver glycogen-targeting subunit (GL) of protein phosphatase 1 (PP1) have identified three separate domains that are responsible for binding of PP1, glycogen and phosphorylase a. The glycogen-binding domain spans the centre of GL between residues 144 and 231 and appears to be distinct from the glycogen-binding (storage) site of phosphorylase. The regulatory high-affinity binding site for phosphorylase a lies in the 16 amino acids at the C-terminus of GL. The PP1-binding domain is deduced to comprise the -RVXF- motif [Egloff, Johnson, Moorhead, Cohen and Barford (1997) EMBO J. 16, 1876-1887] located at residues 61-64 of GL and preceding lysine residues at positions 56, 57 and 59. A possible approach for increasing glycogen synthesis in certain disorders is discussed.

PMID:
9841883
PMCID:
PMC1219922
[Indexed for MEDLINE]
Free PMC Article

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