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

Overview

Journal Biochem J

Specialty Biochemistry

Date 1998 Dec 8

PMID 9841883

Citations 27

Authors

C G Armstrong

M J Doherty

P T Cohen

Affiliations

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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.

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